Blue copper proteins as a model for investigating electron transfer processes within polypeptide matrices

Biophysical Chemistry

Volumn 50, Issue 1-2, 1994, Pages 203-216

  Farver, O ^a   Pecht, I ^b  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Ascorbate oxidase; Azurin; Pathway calculation; Pulse radiolysis

Indexed keywords

ASCORBATE OXIDASE; AZURIN;

CONFERENCE PAPER; ELECTRON TRANSPORT; PRIORITY JOURNAL; PULSE RADIOLYSIS;

ASCORBATE OXIDASE; AZURIN; BACTERIAL PROTEINS; ELECTRON TRANSPORT; MACROMOLECULAR SYSTEMS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; OXIDATION-REDUCTION; PROTEIN CONFORMATION; SUPPORT, NON-U.S. GOV'T;

EID: 0028273042     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/0301-4622(94)85032-1     Document Type: Article

References (46)

1. Long Range Electron Transfer in Biology
2. Electron Transfer in Supermolecules
3. Copper coordination geometry in azurin undergoes minimal change on reduction of copper(II) to copper(I)
4. Photoinduced electron transfer in ruthenium-modified cytochrome c
5. Ascorbate Oxidase: Molecular Properties and Catalytic Activity
6. Long Range Electron Transfer in Blue Copper Proteins
7. Low activation barriers characterize intramolecular electron transfer in ascorbate oxidase.
8. Pulse-radiolysis studies on the oxidised form of the multicopper enzyme ascorbate oxidase: evidence for two intramolecular electron-transfer steps