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Article

Stopped-Flow Studies of the Reduction of the Copper Centers Suggest a Bifurcated Electron Transfer Pathway in Peptidylglycine Monooxygenase.

Biochemistry - 5 Apr 2016

Chauhan Shefali, Hosseinzadeh Parisa, Lu Yi, Blackburn Ninian J

Abstract excerpt

Peptidylglycine monooxygenase (PHM) is a dicopper enzyme that plays a vital role in the amidation of glycine-extended pro-peptides. One of the crucial aspects of its chemistry is the transfer of two electrons from an electron-storing and -transferring site (CuH) to the oxygen binding site and catalytic center (CuM) over a distance of 11 Å during one catalytic turnover event. Here we present our studies of the...

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Identifiers

PMID: 26982589
DOI: 10.1021/acs.biochem.6b00061
PMCID: PMC4879618

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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