The proportion of Met80-sulfoxide dictates peroxidase activity of human cytochrome c-Reference-Cited by-同舟云学术

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The proportion of Met80-sulfoxide dictates peroxidase activity of human cytochrome c

Published:2018 Issue:27 Volume:47 Page:9128-9135
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Parakra Rinky D.¹²³⁴⁵,Kleffmann Torsten¹²³⁴⁵^ORCID,Jameson Guy N. L.⁶⁷⁸⁹¹⁰^ORCID,Ledgerwood Elizabeth C.¹²³⁴⁵^ORCID

Affiliation:

1. Department of Biochemistry

2. School of Biomedical Sciences

3. University of Otago

4. Dunedin 9054

5. New Zealand

6. School of Chemistry

7. Bio21 Molecular Science and Biotechnology Institute

8. 30 Flemington Road

9. The University of Melbourne

10. Parkville

Abstract

Peroxidase activity of cytochrome c is activated and deactivated by methionine 80 oxidation to the sulfoxide and sulfone respectively.

Funder

University of Otago

University of Melbourne

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/DT/C8DT02185F

Reference36 articles.

1. Cytochrome c: Occurrence and Functions

2. Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination

3. A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia

4. Multifunctional Cytochrome c: Learning New Tricks from an Old Dog

5. Alternative Conformations of Cytochrome c: Structure, Function, and Detection

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