Literature DB >> 6258649

Interactions of cytochrome aa3 with oxygen and carbon monoxide. The role of the 607 nm complex.

P Nicholls, G A Chanady.   

Abstract

The 607 nm complex of cytochrome c oxidase, formed aerobically in the presence of CO, appears as an intermediate during the oxidation of CO to CO2 by the enzyme. Maximal steady-state formation of this complex requires oxygen, high levels of carbon monoxide, and the presence of an endogenous hydrogen donor system or the addition of small amounts of reductant (both with isolated enzyme and mitochondrial preparations). The 607 nm complex can be formed after removing CO from the mixed-valence CO complex (cytochrome a3+a2(3)+CO) by aerating the presumably CO-free product. The elements of CO are, therefore, probably not part of the 607 nm complex nor of the related "compound C" produced at low temperatures.

Entities:  

Mesh:

Substances:

Year:  1981        PMID: 6258649     DOI: 10.1016/0005-2728(81)90144-4

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  6 in total

1.  Redox transitions between oxygen intermediates in cytochrome-c oxidase.

Authors:  M I Verkhovsky; J E Morgan; M Wikström
Journal:  Proc Natl Acad Sci U S A       Date:  1996-10-29       Impact factor: 11.205

2.  Interconversions of P and F intermediates of cytochrome c oxidase from Paracoccus denitrificans.

Authors:  Iris von der Hocht; Jessica H van Wonderen; Florian Hilbers; Heike Angerer; Fraser MacMillan; Hartmut Michel
Journal:  Proc Natl Acad Sci U S A       Date:  2011-02-22       Impact factor: 11.205

3.  Formation and reduction of a 'peroxy' intermediate of cytochrome c oxidase by hydrogen peroxide.

Authors:  J M Wrigglesworth
Journal:  Biochem J       Date:  1984-02-01       Impact factor: 3.857

Review 4.  Reactivity of nitric oxide with cytochrome c oxidase: interactions with the binuclear centre and mechanism of inhibition.

Authors:  J Torres; C E Cooper; M Sharpe; M T Wilson
Journal:  J Bioenerg Biomembr       Date:  1998-02       Impact factor: 2.945

5.  Spectroscopic evidence for the participation of compound A (Fea32+-O2) in the reaction of mixed-valence cytochrome c oxidase with oxygen at room temperature.

Authors:  B C Hill; C Greenwood
Journal:  Biochem J       Date:  1983-12-01       Impact factor: 3.857

6.  Cytochrome bo from Escherichia coli: reaction of the oxidized enzyme with hydrogen peroxide.

Authors:  N J Watmough; M R Cheesman; C Greenwood; A J Thomson
Journal:  Biochem J       Date:  1994-06-01       Impact factor: 3.857

  6 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.