Ferroprotoporphyrin IX (BioDeep_00000910928)

   


代谢物信息卡片


Ferroprotoporphyrin IX

化学式: C34H32FeN4O4-2 (616.1772821999999)
中文名称:
谱图信息: 最多检出来源 Homo sapiens(blood) 83.33%

分子结构信息

SMILES: CC1=C(C2=CC3=NC(=CC4=C(C(=C([N-]4)C=C5C(=C(C(=N5)C=C1[N-]2)C=C)C)C=C)C)C(=C3CCC(=O)O)C)CCC(=O)O.[Fe]
InChI: /p-2

描述信息

同义名列表

1 个代谢物同义名

Ferroprotoporphyrin IX



数据库引用编号

3 个数据库交叉引用编号

分类词条

相关代谢途径

Reactome(47)

BioCyc(25)

PlantCyc(1)

代谢反应

479 个相关的代谢反应过程信息。

Reactome(340)

BioCyc(22)

  • heme degradation I: H+ + O2 + a reduced [NADPH-hemoprotein reductase] + ferroheme b ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized [NADPH-hemoprotein reductase]
  • heme degradation IV: A + H+ + O2 + ferroheme b + hydrogen peroxide ⟶ A(H2) + CO + Fe3+ + hematinate + tripyrrole
  • heme degradation III: A(H2) + H+ + O2 + ferroheme b ⟶ A + CO + Fe2+ + H2O + biliverdin-IX δ
  • heme degradation II: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + ferroheme b ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • heme degradation I: H+ + O2 + a reduced [NADPH-hemoprotein reductase] + ferroheme b ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized [NADPH-hemoprotein reductase]
  • phycoerythrobilin biosynthesis II: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + ferroheme b ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phycoviolobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + ferroheme b ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phycoerythrobilin biosynthesis I: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + ferroheme b ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phycourobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + ferroheme b ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + ferroheme b ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phycocyanobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + ferroheme b ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • heme degradation VI: A(H2) + H+ + O2 + ferroheme b ⟶ β-staphylobilin + A + Fe2+ + H2O + formaldehyde
  • heme degradation VI: A(H2) + H+ + O2 + ferroheme b ⟶ δ-staphylobilin + A + Fe2+ + H2O + formaldehyde
  • heme biosynthesis: O2 + protoporphyrinogen IX ⟶ hydrogen peroxide + protoporphyrin IX
  • heme biosynthesis from uroporphyrinogen-III II: H+ + uroporphyrinogen-III ⟶ CO2 + coproporphyrinogen III
  • heme degradation V: δ-anaerubin + NADP+ ⟶ H+ + NADPH + anaerobilin
  • heme degradation VII: A(H2) + H+ + O2 + ferroheme b ⟶ A + Fe2+ + H2O + mycobilin b
  • heme degradation VII: A(H2) + H+ + O2 + ferroheme b ⟶ A + Fe2+ + H2O + mycobilin b
  • heme b biosynthesis IV (Gram-positive bacteria): H+ + harderoheme III + hydrogen peroxide ⟶ CO2 + H2O + ferroheme b
  • heme b biosynthesis IV (Gram-positive bacteria): H+ + coproheme III + hydrogen peroxide ⟶ CO2 + H2O + harderoheme III
  • heme b biosynthesis III (from siroheme): 12,18-didecarboxysiroheme + A(H2) + SAM ⟶ 5'-deoxyadenosine + A + H+ + acetate + coproheme III + met
  • heme biosynthesis III (from siroheme): 12,18-didecarboxysiroheme + A(H2) + SAM ⟶ 5'-deoxyadenosine + A + Fe-coproporphyrin III + H+ + acetate + met

WikiPathways(1)

Plant Reactome(0)

INOH(0)

PlantCyc(116)

  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • heme degradation I: H+ + O2 + a reduced [NADPH-hemoprotein reductase] + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized [NADPH-hemoprotein reductase]
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • heme degradation I: H+ + O2 + a reduced [NADPH-hemoprotein reductase] + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized [NADPH-hemoprotein reductase]
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • heme degradation I: H+ + O2 + a reduced [NADPH-hemoprotein reductase] + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized [NADPH-hemoprotein reductase]
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • heme degradation I: H+ + O2 + a reduced [NADPH-hemoprotein reductase] + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized [NADPH-hemoprotein reductase]
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • heme degradation I: H+ + O2 + a reduced [NADPH-hemoprotein reductase] + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized [NADPH-hemoprotein reductase]
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster
  • phytochromobilin biosynthesis: H+ + O2 + a reduced ferredoxin [iron-sulfur] cluster + protoheme ⟶ (Z,Z)-biliverdin-IX α + CO + Fe2+ + H2O + an oxidized ferredoxin [iron-sulfur] cluster

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0 个相关的物种来源信息

在这里通过桑基图来展示出与当前的这个代谢物在我们的BioDeep知识库中具有相关联信息的其他代谢物。在这里进行关联的信息来源主要有：

  • PubMed: 来源于PubMed文献库中的文献信息，我们通过自然语言数据挖掘得到的在同一篇文献中被同时提及的相关代谢物列表，这个列表按照代谢物同时出现的文献数量降序排序，取前10个代谢物作为相关研究中关联性很高的代谢物集合展示在桑基图中。
  • NCBI Taxonomy: 通过文献数据挖掘，得到的代谢物物种来源信息关联。这个关联信息同样按照出现的次数降序排序，取前10个代谢物作为高关联度的代谢物集合展示在桑吉图上。
  • Chemical Taxonomy: 在物质分类上处于同一个分类集合中的其他代谢物
  • Chemical Reaction: 在化学反应过程中，存在为当前代谢物相关联的生化反应过程中的反应底物或者反应产物的关联代谢物信息。

点击图上的相关代谢物的名称，可以跳转到相关代谢物的信息页面。



文献列表

  • Suriya Palamae, Wattana Temdee, Jirakrit Saetang, Umesh Patil, Watcharapol Suyapoh, Mingkwan Yingkajorn, Xinru Fan, Bin Zhang, Soottawat Benjakul. Impact of high-pressure processing on hemolymph, color, lipid globular structure and oxidation of the edible portion of blood clams. Food chemistry. 2024 Jul; 447(?):138948. doi: 10.1016/j.foodchem.2024.138948. [PMID: 38513490]
  • Mohd Junaid Wani, Amin Arif, Khushtar Anwar Salman, Riaz Mahmood. Glycated LDL generates reactive species that damage cell components, oxidize hemoglobin and alter surface morphology in human erythrocytes. International journal of biological macromolecules. 2024 Jun; 269(Pt 2):132257. doi: 10.1016/j.ijbiomac.2024.132257. [PMID: 38729492]
  • Ana Beatriz Walter-Nuno, Mabel Taracena-Agarwal, Matheus P Oliveira, Marcus F Oliveira, Pedro L Oliveira, Gabriela O Paiva-Silva. Export of heme by the feline leukemia virus C receptor regulates mitochondrial biogenesis and redox balance in the hematophagous insect Rhodnius prolixus. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2024 May; 38(10):e23691. doi: 10.1096/fj.202301671rr. [PMID: 38780525]
  • Yogesh Dubey, Shabnam Mansuri, Sriram Kanvah. Detecting labile heme and ferroptosis through 'turn-on' fluorescence and lipid droplet localization post Fe2+ sensing. Journal of materials chemistry. B. 2024 May; 12(20):4962-4974. doi: 10.1039/d4tb00353e. [PMID: 38687117]
  • Nicolas Grosjean, Estella F Yee, Desigan Kumaran, Kriti Chopra, Macon Abernathy, Sandeep Biswas, James Byrnes, Dale F Kreitler, Jan-Fang Cheng, Agnidipta Ghosh, Steven C Almo, Masakazu Iwai, Krishna K Niyogi, Himadri B Pakrasi, Ritimukta Sarangi, Hubertus van Dam, Lin Yang, Ian K Blaby, Crysten E Blaby-Haas. A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria. Nature communications. 2024 Apr; 15(1):3167. doi: 10.1038/s41467-024-47486-z. [PMID: 38609367]
  • Cleverson D T Freitas, José H Costa, Thais A Germano, Raquel de O Rocha, Márcio V Ramos, Leandro P Bezerra. Class III plant peroxidases: From classification to physiological functions. International journal of biological macromolecules. 2024 Apr; 263(Pt 1):130306. doi: 10.1016/j.ijbiomac.2024.130306. [PMID: 38387641]
  • Min Cui, Hao Wu, Hanmo Zhang, Liping Wei, Xin Qi. Associations of dietary iron intake with cardiovascular disease risk and dyslipidemia among Chinese adults. Lipids in health and disease. 2024 Mar; 23(1):67. doi: 10.1186/s12944-024-02058-4. [PMID: 38431652]
  • William W Parson, Jingcheng Huang, Martin Kulke, Josh V Vermaas, David M Kramer. Electron transfer in a crystalline cytochrome with four hemes. The Journal of chemical physics. 2024 Feb; 160(6):. doi: 10.1063/5.0186958. [PMID: 38341797]
  • Yunzhi Liu, Junrong Xu, Xuefang Lu, Mengxiao Huang, Yuanzhi Mao, Chuanghao Li, Wenjin Yu, Changxia Li. Carbon monoxide is involved in melatonin-enhanced drought resistance in tomato seedlings by enhancing chlorophyll synthesis pathway. BMC plant biology. 2024 Feb; 24(1):97. doi: 10.1186/s12870-024-04793-3. [PMID: 38331770]
  • Chen-Song Dong, Wei-Lun Zhang, Xiao-Ying Wang, Xiao Wang, Jia Wang, Mingzhu Wang, Ying Fang, Lin Liu. Crystallographic and functional studies of a plant temperature-induced lipocalin. Biochimica et biophysica acta. General subjects. 2024 Feb; 1868(2):130540. doi: 10.1016/j.bbagen.2023.130540. [PMID: 38103756]
  • Marta Manco, Giorgia Ammirata, Sara Petrillo, Francesco De Giorgio, Simona Fontana, Chiara Riganti, Paolo Provero, Sharmila Fagoonee, Fiorella Altruda, Emanuela Tolosano. FLVCR1a Controls Cellular Cholesterol Levels through the Regulation of Heme Biosynthesis and Tricarboxylic Acid Cycle Flux in Endothelial Cells. Biomolecules. 2024 Jan; 14(2):. doi: 10.3390/biom14020149. [PMID: 38397386]
  • Yang Gu, Ziying Li, Han Li, Xiaoling Yi, Xun Liu, Yan Zhang, Shu Gong, Tao Yu, Li Li. Exploring the efficacious constituents and underlying mechanisms of sini decoction for sepsis treatment through network pharmacology and multi-omics. Phytomedicine : international journal of phytotherapy and phytopharmacology. 2024 Jan; 123(?):155212. doi: 10.1016/j.phymed.2023.155212. [PMID: 38029626]
  • Kristen S Hill, Erin E Schuler, Sally R Ellingson, Jill M Kolesar. Artesunate acts through cytochrome c to inhibit growth of pediatric AML cells. Scientific reports. 2023 12; 13(1):22383. doi: 10.1038/s41598-023-49928-y. [PMID: 38104159]
  • Huihui Liu, Qing Wang, Jingru Guo, Kai Feng, Yiling Ruan, Zhihao Zhang, Xin Ji, Jigang Wang, Tao Zhang, Xiaolian Sun. Prodrug-based strategy with a two-in-one liposome for Cerenkov-induced photodynamic therapy and chemotherapy. Journal of controlled release : official journal of the Controlled Release Society. 2023 12; 364(?):206-215. doi: 10.1016/j.jconrel.2023.10.036. [PMID: 37884209]
  • Dipun Nirmal Perera, Chathurangi Lakshika Palliyaguruge, Dasuni Dilkini Eapasinghe, Dilmi Maleesha Liyanage, R A C Haily Seneviratne, S M D Demini, J A S M Jayasinghe, Mishal Faizan, Umapriyatharshini Rajagopalan, B Prasanna Galhena, Hasi Hays, Kanishka Senathilake, Kamani H Tennekoon, Sameera R Samarakoon. Factors affecting iron absorption and the role of fortification in enhancing iron levels. Nutrition bulletin. 2023 Nov; ?(?):. doi: 10.1111/nbu.12643. [PMID: 37965925]
  • Pauline Puylaert, Lynn Roth, Melissa Van Praet, Isabel Pintelon, Catalina Dumitrascu, Alexander van Nuijs, Greta Klejborowska, Pieter-Jan Guns, Tom Vanden Berghe, Koen Augustyns, Guido R Y De Meyer, Wim Martinet. Effect of erythrophagocytosis-induced ferroptosis during angiogenesis in atherosclerotic plaques. Angiogenesis. 2023 11; 26(4):505-522. doi: 10.1007/s10456-023-09877-6. [PMID: 37120604]
  • Qianwen Guo, Ziyue Yin, Junfei Cheng, Xiaojing Zhang, Rong Wang, Wenbin Li. Protective effect of heme chloride on hypoxia-induced tissue injury in mice. Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences. 2023 Oct; 48(10):1437-1444. doi: 10.11817/j.issn.1672-7347.2023.230204. [PMID: 38432874]
  • Agris Pentjuss, Emils Bolmanis, Anastasija Suleiko, Elina Didrihsone, Arturs Suleiko, Konstantins Dubencovs, Janis Liepins, Andris Kazaks, Juris Vanags. Pichia pastoris growth-coupled heme biosynthesis analysis using metabolic modelling. Scientific reports. 2023 09; 13(1):15816. doi: 10.1038/s41598-023-42865-w. [PMID: 37739976]
  • Sandra Rayego-Mateos, José Luis Morgado-Pascual, Cristina García-Caballero, Iolanda Lazaro, Aleix Sala-Vila, Lucas Opazo-Rios, Sebastian Mas-Fontao, Jesús Egido, Marta Ruiz-Ortega, Juan Antonio Moreno. Intravascular hemolysis triggers NAFLD characterized by a deregulation of lipid metabolism and lipophagy blockade. The Journal of pathology. 2023 Aug; ?(?):. doi: 10.1002/path.6161. [PMID: 37555366]
  • Li Feng, Lijuan Wei, Yayu Liu, Jiaxuan Ren, Weibiao Liao. Carbon monoxide/heme oxygenase system in plant: Roles in abiotic stress response and crosstalk with other signals molecules. Nitric oxide : biology and chemistry. 2023 Jun; 138-139(?):51-63. doi: 10.1016/j.niox.2023.06.005. [PMID: 37364740]
  • G P Coló, K Schweitzer, G M Oresti, E G Alonso, L Fernández Chávez, M Mascaró, G Giorgi, A C Curino, M M Facchinetti. Proteomic analysis of the effect of hemin in breast cancer. Scientific reports. 2023 06; 13(1):10091. doi: 10.1038/s41598-023-35125-4. [PMID: 37344532]
  • Zarmin Iqbal, Ruhul Quds, Riaz Mahmood. Vanillin attenuates CdCl2-induced cytotoxicity in isolated human erythrocytes. Toxicology in vitro : an international journal published in association with BIBRA. 2023 Jun; ?(?):105633. doi: 10.1016/j.tiv.2023.105633. [PMID: 37336463]
  • Kazuya Ishikawa, Xiaonan Xie, Yasuhide Osaki, Atsushi Miyawaki, Keiji Numata, Yutaka Kodama. Bilirubin is produced nonenzymatically in plants to maintain chloroplast redox status. Science advances. 2023 06; 9(23):eadh4787. doi: 10.1126/sciadv.adh4787. [PMID: 37285441]
  • Chinmay Dey, Madhuparna Roy, Abhishek Dey, Somdatta Ghosh Dey. Heme-Aβ in SDS micellar environment: Active site environment and reactivity. Journal of inorganic biochemistry. 2023 Jun; 246(?):112271. doi: 10.1016/j.jinorgbio.2023.112271. [PMID: 37301164]
  • Peng Lv, Feng Liu. Heme-deficient primitive red blood cells induce HSPC ferroptosis by altering iron homeostasis during zebrafish embryogenesis. Development (Cambridge, England). 2023 May; ?(?):. doi: 10.1242/dev.201690. [PMID: 37227070]
  • Andrés Álvarez-Armenta, David O Corona-Martínez, Ramón Pacheco-Aguilar, Alonso A López-Zavala, Rogerio R Sotelo-Mundo, Guillermina García-Sánchez, Juan Carlos Ramírez-Suárez. Sulfmyoglobin production by free cysteine during thermal treatment: Involvement of heme iron in the production of free radicals. Food chemistry. 2023 May; 408(?):135165. doi: 10.1016/j.foodchem.2022.135165. [PMID: 36527926]
  • Tingting Fan, Lena Roling, Boris Hedtke, Bernhard Grimm. FC2 stabilizes POR and suppresses ALA formation in the tetrapyrrole biosynthesis pathway. The New phytologist. 2023 May; ?(?):. doi: 10.1111/nph.18952. [PMID: 37161708]
  • Cengiz Kaya, Muhammed Ashraf, Mohammed Nasser Alyemeni, Jörg Rinklebe, Parvaiz Ahmad. Alleviation of arsenic toxicity in pepper plants by aminolevulinic acid and heme through modulating its sequestration and distribution within cell organelles. Environmental pollution (Barking, Essex : 1987). 2023 May; ?(?):121747. doi: 10.1016/j.envpol.2023.121747. [PMID: 37146870]
  • Bixia Zhang, Jacob A Lewis, Wilfred Vermerris, Scott E Sattler, ChulHee Kang. A sorghum ascorbate peroxidase with four binding sites has activity against ascorbate and phenylpropanoids. Plant physiology. 2023 05; 192(1):102-118. doi: 10.1093/plphys/kiac604. [PMID: 36575825]
  • November Sankey, Haley Merrick, Padam Singh, Janet Rogers, Amit Reddi, Steven D Hartson, Avishek Mitra. Role of the Mycobacterium tuberculosis ESX-4 Secretion System in Heme Iron Utilization and Pore Formation by PPE Proteins. mSphere. 2023 04; 8(2):e0057322. doi: 10.1128/msphere.00573-22. [PMID: 36749044]
  • David Stucki, Philipp Westhoff, Dominik Brilhaus, Andreas P M Weber, Peter Brenneisen, Wilhelm Stahl. Carbon monoxide exposure activates ULK1 via AMPK phosphorylation in murine embryonic fibroblasts. International journal for vitamin and nutrition research. Internationale Zeitschrift fur Vitamin- und Ernahrungsforschung. Journal international de vitaminologie et de nutrition. 2023 Apr; 93(2):122-131. doi: 10.1024/0300-9831/a000714. [PMID: 34074127]
  • Minghao Ma, Ruixia Wang, Ming Xu. Thorium(IV) triggers ferroptosis through disrupting iron homeostasis and heme metabolism in the liver following oral ingestion. Journal of hazardous materials. 2023 Mar; 452(?):131217. doi: 10.1016/j.jhazmat.2023.131217. [PMID: 36940529]
  • Weiyu Chen, Sergey Tumanov, Christopher P Stanley, Stephanie M Y Kong, James Nadel, Niv Vigder, Darren Newington, Xiaosuo Wang, Louise L Dunn, Roland Stocker. Destabilization of Atherosclerotic Plaque by Bilirubin Deficiency. Circulation research. 2023 Mar; ?(?):. doi: 10.1161/circresaha.122.322418. [PMID: 36876485]
  • Lu Liu, Zongshan Zhang, Hui Liu, Shengnan Zhu, Taoxun Zhou, Chunqun Wang, Min Hu. Identification and characterisation of the haemozoin of Haemonchus contortus. Parasites & vectors. 2023 Mar; 16(1):88. doi: 10.1186/s13071-023-05714-3. [PMID: 36879311]
  • Sherif Elsabbagh, Marius Landau, Harald Gross, Anita Schultz, Joachim E Schultz. Heme b inhibits class III adenylyl cyclases. Cellular signalling. 2023 Mar; 103(?):110568. doi: 10.1016/j.cellsig.2022.110568. [PMID: 36565898]
  • Joo-Yeun Oh, Marisa B Marques, Xin Xu, Jindong Li, Kristopher R Genschmer, Edward Phillips, Melissa F Chimento, James Mobley, Amit Gaggar, Rakesh P Patel. Different-sized extracellular vesicles derived from stored red blood cells package diverse cargoes and cause distinct cellular effects. Transfusion. 2023 03; 63(3):586-600. doi: 10.1111/trf.17271. [PMID: 36752125]
  • Zhenzhao Li, Minh Ha, Damian Frank, Melindee Hastie, Robyn D Warner. Muscle fibre type composition influences the formation of odour-active volatiles in beef. Food research international (Ottawa, Ont.). 2023 03; 165(?):112468. doi: 10.1016/j.foodres.2023.112468. [PMID: 36869481]
  • Jenny U Tran, Breann L Brown. The yeast ALA synthase C-terminus positively controls enzyme structure and function. Protein science : a publication of the Protein Society. 2023 Feb; ?(?):e4600. doi: 10.1002/pro.4600. [PMID: 36807942]
  • Robert H Calderon, Catherine de Vitry, Francis-André Wollman, Krishna K Niyogi. Rubredoxin 1 promotes the proper folding of D1 and is not required for heme b559 assembly in Chlamydomonas photosystem II. The Journal of biological chemistry. 2023 Feb; ?(?):102968. doi: 10.1016/j.jbc.2023.102968. [PMID: 36736898]
  • Andreas S Richter, Thomas Nägele, Bernhard Grimm, Kerstin Kaufmann, Michael Schroda, Dario Leister, Tatjana Kleine. Retrograde signaling in plants: A critical review focusing on the GUN pathway and beyond. Plant communications. 2023 01; 4(1):100511. doi: 10.1016/j.xplc.2022.100511. [PMID: 36575799]
  • R Luong, R V Ribeiro, A Rangan, V Naganathan, F Blyth, L M Waite, D J Handelsman, D G Le Couteur, M J Seibel, V Hirani. Haem Iron Intake Is Associated with Increased Major Adverse Cardiovascular Events, All-Cause Mortality, Congestive Cardiac Failure, and Coronary Revascularisation in Older Men: The Concord Health and Ageing in Men Project. The journal of nutrition, health & aging. 2023; 27(7):559-570. doi: 10.1007/s12603-023-1945-6. [PMID: 37498103]
  • Diana Humer, Julian Ebner. The Purification of Heme Peroxidases from Escherichia coli Inclusion Bodies: A Success Story Shown by the Example of Horseradish Peroxidase. Methods in molecular biology (Clifton, N.J.). 2023; 2617(?):227-237. doi: 10.1007/978-1-0716-2930-7_16. [PMID: 36656528]
  • Ryoya Kohata, HyunSeok Lim, Yuki Kanamoto, Akio Murakami, Yuichi Fujita, Ayumi Tanaka, Wesley Swingley, Hisashi Ito, Ryouichi Tanaka. Heterologous complementation systems verify the mosaic distribution of three distinct protoporphyrinogen IX oxidase in the cyanobacterial phylum. Journal of plant research. 2023 Jan; 136(1):107-115. doi: 10.1007/s10265-022-01423-7. [PMID: 36357749]
  • Shengjie Liao, Mi Huang, Yanli Liao, Chao Yuan. HMOX1 Promotes Ferroptosis Induced by Erastin in Lens Epithelial Cell through Modulates Fe2+ Production. Current eye research. 2023 01; 48(1):25-33. doi: 10.1080/02713683.2022.2138450. [PMID: 36300537]
  • Jinjing Xu, Kuiyang Zhu, Yali Wang, Jing Chen. The dual role and mutual dependence of heme/HO-1/Bach1 axis in the carcinogenic and anti-carcinogenic intersection. Journal of cancer research and clinical oncology. 2023 Jan; 149(1):483-501. doi: 10.1007/s00432-022-04447-7. [PMID: 36310300]
  • Eerappa Rajakumara, Dubey Saniya, Priyanka Bajaj, Rajanna Rajeshwari, Jyotsnendu Giri, Mehdi D Davari. Hijacking Chemical Reactions of P450 Enzymes for Altered Chemical Reactions and Asymmetric Synthesis. International journal of molecular sciences. 2022 Dec; 24(1):. doi: 10.3390/ijms24010214. [PMID: 36613657]
  • Mengyang Liu, Wei Ma, Xiangjie Su, Xiaomeng Zhang, Yin Lu, Shaowei Zhang, Jinghui Yan, Daling Feng, Lisong Ma, Aoife Taylor, Yunjia Ge, Qi Cheng, Kedong Xu, Yanhua Wang, Na Li, Aixia Gu, Ju Zhang, Shuangxia Luo, Shuxin Xuan, Xueping Chen, Nigel S Scrutton, Chengwei Li, Jianjun Zhao, Shuxing Shen. Mutation in a chlorophyll-binding motif of Brassica ferrochelatase enhances both heme and chlorophyll biosynthesis. Cell reports. 2022 12; 41(10):111758. doi: 10.1016/j.celrep.2022.111758. [PMID: 36476857]
  • Dan Dang, Zhaoli Meng, Chuan Zhang, Zhenyu Li, Jiaqi Wei, Hui Wu. Heme induces intestinal epithelial cell ferroptosis via mitochondrial dysfunction in transfusion-associated necrotizing enterocolitis. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2022 12; 36(12):e22649. doi: 10.1096/fj.202200853rrr. [PMID: 36383399]
  • Xiaojing Qian, Huifang Chen, Jiaying Chen. Preventing heme-induced nephropathy in children with glucose 6 phosphate dehydrogenase deficiency: is there a role for acetazolamide?. Pediatric nephrology (Berlin, Germany). 2022 12; 37(12):3249. doi: 10.1007/s00467-022-05642-x. [PMID: 35678880]
  • Debakshi Mullick, Katya Rechav, Leslie Leiserowitz, Neta Regev-Rudzki, Ron Dzikowski, Michael Elbaum. Diffraction contrast in cryo-scanning transmission electron tomography reveals the boundary of hemozoin crystals in situ. Faraday discussions. 2022 11; 240(0):127-141. doi: 10.1039/d2fd00088a. [PMID: 35938388]
  • Pedro G Vásquez-Ocmín, Jean-François Gallard, Anne-Cécile Van Baelen, Karine Leblanc, Sandrine Cojean, Elisabeth Mouray, Philippe Grellier, Carlos A Amasifuén Guerra, Mehdi A Beniddir, Laurent Evanno, Bruno Figadère, Alexandre Maciuk. Biodereplication of Antiplasmodial Extracts: Application of the Amazonian Medicinal Plant Piper coruscans Kunth. Molecules (Basel, Switzerland). 2022 Nov; 27(21):. doi: 10.3390/molecules27217638. [PMID: 36364460]
  • Ko Abe, Masataka Ikeda, Tomomi Ide, Tomonori Tadokoro, Hiroko Deguchi Miyamoto, Shun Furusawa, Yoshitomo Tsutsui, Ryo Miyake, Kosei Ishimaru, Masatsugu Watanabe, Shouji Matsushima, Tomoko Koumura, Ken-Ichi Yamada, Hirotaka Imai, Hiroyuki Tsutsui. Doxorubicin causes ferroptosis and cardiotoxicity by intercalating into mitochondrial DNA and disrupting Alas1-dependent heme synthesis. Science signaling. 2022 11; 15(758):eabn8017. doi: 10.1126/scisignal.abn8017. [PMID: 36318618]
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