Investigation of the pathway for inter-copper electron transfer in peptidylglycine alpha-amidating monooxygenase.
Peptidylglycine alpha-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.
Francisco
Wilson A
WA
Department of Chemistry, University of California, Berkeley, Berkeley, California 94720-1460, USA.
Wille
Georg
G
Smith
Alan J
AJ
Merkler
David J
DJ
Klinman
Judith P
JP
D003300:Copper / Q000737:chemistry* / Q000378:metabolism*; D004299:Dopamine beta-Hydroxylase / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D013816:Thermodynamics
D009097:Multienzyme Complexes; D003300:Copper; D006899:Mixed Function Oxygenases; D004299:Dopamine beta-Hydroxylase; C035189:peptidylglycine monooxygenase