Investigation of the pathway for inter-copper electron transfer in peptidylglycine α-amidating monooxygenase

Wilson A. Francisco, Georg Wille, Alan J. Smith, David J. Merkler, Judith P. Klinman

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

Peptidylglycine α-amidating monooxygenase catalyzes the oxidative cleavage of glycine extended peptides at their terminus. In the course of the reaction, there is a requisite long-range electron transfer between the two copper centers (CuH and CuM) located in the hydroxylating domain. This communication presents data that argue against the participation of the extended peptide backbone of substrate in the long-range electron transfer. We propose that electron transfer occurs via the bulk solvent that separates CuH from CuM.

Original languageEnglish (US)
Pages (from-to)13168-13169
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number41
DOIs
StatePublished - Oct 20 2004

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Mixed Function Oxygenases
Copper
Electrons
Peptides
Glycine
Amino acids
Communication
Substrates
peptidylglycine monooxygenase

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Investigation of the pathway for inter-copper electron transfer in peptidylglycine α-amidating monooxygenase. / Francisco, Wilson A.; Wille, Georg; Smith, Alan J.; Merkler, David J.; Klinman, Judith P.

In: Journal of the American Chemical Society, Vol. 126, No. 41, 20.10.2004, p. 13168-13169.

Research output: Contribution to journalArticle

Francisco, Wilson A. ; Wille, Georg ; Smith, Alan J. ; Merkler, David J. ; Klinman, Judith P. / Investigation of the pathway for inter-copper electron transfer in peptidylglycine α-amidating monooxygenase. In: Journal of the American Chemical Society. 2004 ; Vol. 126, No. 41. pp. 13168-13169.
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