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The role of arginine-127 at the proximal NO-binding site in determining the electronic structure and function of 5-coordinate NO-heme in cytochrome c' of Rhodobacter sphaeroides.

Abstract:

Cytochrome c' is a heme protein from a denitrifying variant of Rhodobacter sphaeroides which may serve to store and transport metabolic NO while protecting against NO toxicity. Its heme site bears resemblance through its 5-coordinate NO-binding capability to the regulatory site in soluble guanylate cyclase. A conserved arginine (Arg-127) abuts the 5-coordinate NO-heme binding site, and the alanine mutant R127A provided insight into the role of the Arg-127 in establishing the electronic struct...

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Publication status:
Published

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Publisher copy:
10.1021/bi900833f

Authors


Grigoryants, VM More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Shapleigh, JP More by this author
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Journal:
Biochemistry
Volume:
48
Issue:
38
Pages:
8985-8993
Publication date:
2009-09-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:360d236c-9e67-4c51-8389-fce10014cf32
Source identifiers:
428058
Local pid:
pubs:428058

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