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

被引：50

作者：

Francisco, WA

Wille, G

Smith, AJ

Merkler, DJ

Klinman, JP ^{[1
]}

机构：

[1] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[3] Stanford Univ, Ctr Med, Prot & Nucl Acid Facil, Stanford, CA 94305 USA

[4] Univ S Florida, Dept Chem, Tampa, FL 33620 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 41期

关键词：

D O I：

10.1021/ja046888z

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. Copyright © 2004 American Chemical Society.

引用

页码：13168 / 13169

页数：2

共 15 条

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