Azot monoksid reduktaza (citohrom c)
Azot monoksid reduktaza (citohrom c) (EC 1.7.2.5, Azot monoksidna reduktaza (citohrom c)) je enzim sa sistematskim imenom azot monoksid:fericitohrom-c oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju:
| Azot monoksid reduktaza (citohrom c) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.7.2.5 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- azotsuboksid + 2 fericitohrom c +H2O 2 azot monoksid + 2 ferocitohrom c + 2 H+
Enzim iz Pseudomonas aeruginosa sadrži dinuklearni centar koji obuhvata nehemni centar gvožđa i hem b3, plus hem c, hem b i kalcijum. Akceptor je citohrom c551.
Reference uredi
- ↑ Hendriks, J., Warne, A., Gohlke, U., Haltia, T., Ludovici, C., Lubben, M. and Saraste, M. (1998). „The active site of the bacterial nitric oxide reductase is a dinuclear iron center”. Biochemistry 37: 13102-13109. PMID 9748316.
- ↑ Hendriks, J., Gohlke, U. and Saraste, M. (1998). „From NO to OO: nitric oxide and dioxygen in bacterial respiration”. J. Bioenerg. Biomembr. 30: 15-24. PMID 9623801.
- ↑ Heiss, B., Frunzke, K. and Zumpft, W.G. (1989). „Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri”. J. Bacteriol. 171: 3288-3297. PMID 2542222.
- ↑ Cheesman, M.R., Zumft, W.G. and Thomson, A.J. (1998). „The MCD and EPR of the heme centers of nitric oxide reductase from Pseudomonas stutzeri: evidence that the enzyme is structurally related to the heme-copper oxidases”. Biochemistry 37: 3994-4000. PMID 9521721.
- ↑ Kumita, H., Matsuura, K., Hino, T., Takahashi, S., Hori, H., Fukumori, Y., Morishima, I. and Shiro, Y. (2004). „NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: characterization of reaction intermediates that appear in the single turnover cycle”. J. Biol. Chem. 279: 55247-55254. PMID 15504726.
- ↑ Hino, T., Matsumoto, Y., Nagano, S., Sugimoto, H., Fukumori, Y., Murata, T., Iwata, S. and Shiro, Y. (2010). „Structural basis of biological N2O generation by bacterial nitric oxide reductase”. Science 330: 1666-1670. PMID 21109633.
Literatura uredi
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.