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

doi:10.1021/ja046888z

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

Molecular Sciences, School of (SMS)

Research output: Contribution to journal › Article › peer-review

57 Scopus citations

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 (Cu_H and Cu_M) 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 Cu_H from Cu_M.

Original language	English (US)
Pages (from-to)	13168-13169
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	126
Issue number	41
DOIs	https://doi.org/10.1021/ja046888z
State	Published - Oct 20 2004

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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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.",

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AU - Wille, Georg

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AU - Merkler, David J.

AU - Klinman, Judith P.

PY - 2004/10/20

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AB - 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.

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

Abstract

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