PROFILPELAJAR.COM

Ugljen-monoksid dehidrogenaza (citohrom b-561)
Identifikatori
EC broj	1.2.2.4
CAS broj	395639-79-9
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Ugljen-monoksid dehidrogenaza (citohrom b-561) (EC 1.2.2.4, karbon monoksidna oksidaza, karbon monoksidna oksigenaza (citohrom b-561), karbon monoksid:metilnsko plavo oksidoreduktaza, CO dehidrogenaza, karbon-monoksidna dehidrogenaza) je enzim sa sistematskim imenom karbon monoksid, voda:citohrom b-561 oksidoreduktaza.^[1]^[2]^[3]^[4]^[5] Ovaj enzim katalizuje sledeću hemijsku reakciju

CO + H₂O + 2 fericitohrom b-561

\rightleftharpoons

CO₂ + 2 H⁺ + 2 ferocitohrom b-561

Ovaj enzim sadrži molibdopterin citozin dinukleotid, FAD i [2Fe-2S]-klustere. Kiseonik, metilensko plavo I jodonitrotetrazolijum hlorid mogu da deluju kao nefiziološki elektronski akceptori.

Reference

↑ Meyer, O., Jacobitz, S. and Krüger, B. (1986). „Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria”. FEMS Microbiol. Rev. 39: 161-179.
↑ Jacobitz, S. and Meyer, O. (1989). „Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes and restoration of respiratory activities”. J. Bacteriol. 171: 6294-6299. PMID 2808305.
↑ Meyer, O. and Schlegel, H.-G. (1980). „Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans”. J. Bacteriol. 141: 74-80. PMID 7354006.
↑ Dobbek, H., Gremer, L., Meyer, O. and Huber, R. (1999). „Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine”. Proc. Natl. Acad. Sci. USA 96: 8884-8889. PMID 10430865.
↑ Hänzelmann, P., Dobbek, H., Gremer, L., Huber, R. and Meyer, O. (2000). „The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase”. J. Mol. Biol. 301: 1221-1235. PMID 10966817.

Literatura

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.

Vanjske veze

MeSH Carbon-monoxide+dehydrogenase+(cytochrome+b-561)

[1] Meyer, O., Jacobitz, S. and Krüger, B. (1986). „Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria”. FEMS Microbiol. Rev. 39: 161-179.

[2] Jacobitz, S. and Meyer, O. (1989). „Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes and restoration of respiratory activities”. J. Bacteriol. 171: 6294-6299. PMID 2808305.

[3] Meyer, O. and Schlegel, H.-G. (1980). „Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans”. J. Bacteriol. 141: 74-80. PMID 7354006.

[4] Dobbek, H., Gremer, L., Meyer, O. and Huber, R. (1999). „Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine”. Proc. Natl. Acad. Sci. USA 96: 8884-8889. PMID 10430865.

[5] Hänzelmann, P., Dobbek, H., Gremer, L., Huber, R. and Meyer, O. (2000). „The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase”. J. Mol. Biol. 301: 1221-1235. PMID 10966817.

[1]

[2]

[3]

[4]

[5]