Nitric oxide reductase (menaquinol)

↑ Cramm, R., Pohlmann, A. and Friedrich, B. (1999). "Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16". FEBS Lett. 460 (1): 6–10. doi:10.1016/s0014-5793(99)01315-0. PMID 10571051.
↑ Suharti, Strampraad, M.J., Schroder, I. and de Vries, S. (2001). "A novel copper A containing menaquinol NO reductase from Bacillus azotoformans". Biochemistry 40 (8): 2632–2639. doi:10.1021/bi0020067. PMID 11327887.
↑ Suharti, Heering, H.A. and de Vries, S. (2004). "NO reductase from Bacillus azotoformans is a bifunctional enzyme accepting electrons from menaquinol and a specific endogenous membrane-bound cytochrome c₅₅₁". Biochemistry 43 (42): 13487–13495. doi:10.1021/bi0488101. PMID 15491156.

External links

Nitric oxide reductase (menaquinol) at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: nitrogenous donor (EC 1.7)

1.7.1	GMP reductase

1.7.2	Nitrite reductase (NO-forming)

1.7.3	Urate oxidase

1.7.7	Ferredoxin—nitrite reductase

1.7.99	Hydroxylamine reductase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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