Ferriheme a3(1-) (BioDeep_00001054171)
代谢物信息卡片
化学式: C49H60FeN4O6- (856.386201)
中文名称:
谱图信息:
最多检出来源 () 0%
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(CCCC(C)CCCC(C)CCCC(C)C)O)C)C(=C3CCC(=O)[O-])C=O)CCC(=O)[O-].[Fe+3]
InChI: /q
描述信息
A dicarboxylic acid anion obtained by deprotonation of the carboxy groups of ferriheme a3. Major structure at pH 7.3.
同义名列表
1 个代谢物同义名
相关代谢途径
Reactome(0)
BioCyc(0)
PlantCyc(0)
代谢反应
0 个相关的代谢反应过程信息。
Reactome(0)
BioCyc(0)
WikiPathways(0)
Plant Reactome(0)
INOH(0)
PlantCyc(0)
COVID-19 Disease Map(0)
PathBank(0)
PharmGKB(0)
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
- Vivek Sharma, Pablo G Jambrina, Markus Kaukonen, Edina Rosta, Peter R Rich. Insights into functions of the H channel of cytochrome c oxidase from atomistic molecular dynamics simulations.
Proceedings of the National Academy of Sciences of the United States of America.
2017 11; 114(48):E10339-E10348. doi:
10.1073/pnas.1708628114
. [PMID: 29133387] - Takashi Nomura, Sachiko Yanagisawa, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Takashi Ogura. Effects of proton motive force on the structure and dynamics of bovine cytochrome C oxidase in phospholipid vesicles.
Biochemistry.
2014 Oct; 53(40):6382-91. doi:
10.1021/bi501022j
. [PMID: 25231381] - Linda Näsvik Öjemyr, Christoph von Ballmoos, Kristina Faxén, Emelie Svahn, Peter Brzezinski. The membrane modulates internal proton transfer in cytochrome c oxidase.
Biochemistry.
2012 Feb; 51(6):1092-100. doi:
10.1021/bi201795c
. [PMID: 22257086] - Ashtamurthy S Pawate, Joel Morgan, Andreas Namslauer, Denise Mills, Peter Brzezinski, Shelagh Ferguson-Miller, Robert B Gennis. A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping.
Biochemistry.
2002 Nov; 41(45):13417-23. doi:
10.1021/bi026582+
. [PMID: 12416987] - M A Sharpe, C E Cooper. Interaction of peroxynitrite with mitochondrial cytochrome oxidase. Catalytic production of nitric oxide and irreversible inhibition of enzyme activity.
The Journal of biological chemistry.
1998 Nov; 273(47):30961-72. doi:
10.1074/jbc.273.47.30961
. [PMID: 9812992] - K Ikeda, M Toda, K Tanaka, S Tokumaru, S Kojo. Increase of lipid hydroperoxides in liver mitochondria and inhibition of cytochrome oxidase by carbon tetrachloride intoxication in rats.
Free radical research.
1998 Apr; 28(4):403-10. doi:
10.3109/10715769809070809
. [PMID: 9684985] - T Mogi, K Saiki, Y Anraku. Biosynthesis and functional role of haem O and haem A.
Molecular microbiology.
1994 Nov; 14(3):391-8. doi:
10.1111/j.1365-2958.1994.tb02174.x
. [PMID: 7885224] - P A Harmon, R W Hendler, I W Levin. Resonance Raman and optical spectroscopic monitoring of heme a redox states in cytochrome c oxidase during potentiometric titrations.
Biochemistry.
1994 Jan; 33(3):699-707. doi:
10.1021/bi00169a011
. [PMID: 8292597] - B C Hill, L Vo, J Albanese. Kinetic and ligand binding evidence for two heme A-based terminal oxidases in plasma membranes from Bacillus subtilis.
Archives of biochemistry and biophysics.
1993 Feb; 301(1):129-37. doi:
10.1006/abbi.1993.1124
. [PMID: 8382904] - W S Thayer, J J Cummings. Effects of chronic alcohol consumption on the steady-state kinetics properties of cytochrome oxidase in rat liver.
Biochimica et biophysica acta.
1990 Apr; 1016(3):333-8. doi:
10.1016/0005-2728(90)90165-z
. [PMID: 2158817] - J D Weinstein, R Branchaud, S I Beale, W J Bement, P R Sinclair. Biosynthesis of the farnesyl moiety of heme a from exogenous mevalonic acid by cultured chick liver cells.
Archives of biochemistry and biophysics.
1986 Feb; 245(1):44-50. doi:
10.1016/0003-9861(86)90188-8
. [PMID: 3947101]