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Title: Influences of the heme-lysine crosslink in cytochrome P460 over redox catalysis and nitric oxide sensitivity

Abstract

A vital role has been identified for the heme-lysine cross-link unique to cytochromes P460: preventing enzyme deactivation during catalysis by the obligate nitrification metabolite nitric oxide.

Authors:
 [1];  [1]; ORCiD logo [1]
  1. Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, USA
Publication Date:
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1415513
Grant/Contract Number:
AC02-76SF00515; SC0013997
Resource Type:
Journal Article: Published Article
Journal Name:
Chemical Science
Additional Journal Information:
Journal Volume: 9; Journal Issue: 2; Related Information: CHORUS Timestamp: 2018-01-03 13:03:32; Journal ID: ISSN 2041-6520
Publisher:
Royal Society of Chemistry (RSC)
Country of Publication:
United Kingdom
Language:
English

Citation Formats

Vilbert, Avery C., Caranto, Jonathan D., and Lancaster, Kyle M. Influences of the heme-lysine crosslink in cytochrome P460 over redox catalysis and nitric oxide sensitivity. United Kingdom: N. p., 2018. Web. doi:10.1039/C7SC03450D.
Vilbert, Avery C., Caranto, Jonathan D., & Lancaster, Kyle M. Influences of the heme-lysine crosslink in cytochrome P460 over redox catalysis and nitric oxide sensitivity. United Kingdom. doi:10.1039/C7SC03450D.
Vilbert, Avery C., Caranto, Jonathan D., and Lancaster, Kyle M. 2018. "Influences of the heme-lysine crosslink in cytochrome P460 over redox catalysis and nitric oxide sensitivity". United Kingdom. doi:10.1039/C7SC03450D.
@article{osti_1415513,
title = {Influences of the heme-lysine crosslink in cytochrome P460 over redox catalysis and nitric oxide sensitivity},
author = {Vilbert, Avery C. and Caranto, Jonathan D. and Lancaster, Kyle M.},
abstractNote = {A vital role has been identified for the heme-lysine cross-link unique to cytochromes P460: preventing enzyme deactivation during catalysis by the obligate nitrification metabolite nitric oxide.},
doi = {10.1039/C7SC03450D},
journal = {Chemical Science},
number = 2,
volume = 9,
place = {United Kingdom},
year = 2018,
month = 1
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1039/C7SC03450D

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  • No abstract prepared.
  • The authors report that nitric oxide is redox activated by iron(III) porphyrins and heme proteins to a nitrosating species having the character of nitrosonium ion. This reactivity has special significance because it has recently been recognized that the endogenous generation of nitric oxide occurs within a variety of mammalian cell types (21, 22).
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