Spectroscopic and Electrochemical Studies on Active-site Transitions of the Type 1 Copper Protein Pseudoazurin from Achromobacter cycloclastes
Open Access
- 1 October 1995
- journal article
- Published by Elsevier
- Vol. 270 (43) , 25733-25738
- https://doi.org/10.1074/jbc.270.43.25733
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Raman Spectroscopy as an Indicator of Cu-S Bond Length in Type 1 and Type 2 Copper Cysteinate ProteinsJournal of the American Chemical Society, 1994
- Direct Electrochemistry of Nitrite Reductase from Achromobacter cycloclastes IAM 1013Bulletin of the Chemical Society of Japan, 1994
- Active-site electronic structure contributions to electron-transfer pathways in rubredoxin and plastocyanin: direct versus superexchangeJournal of the American Chemical Society, 1993
- Direct electrochemistry of the blue copper proteins pseudoazurin, plantacyanin, and stellacyaninInorganic Chemistry, 1990
- Direct and superexchange electron tunneling at the adjacent and remote sites of higher plant plastocyaninsInorganic Chemistry, 1990
- Crystal structure of plastocyanin from a green alga, Enteromorpha proliferaJournal of Molecular Biology, 1990
- Structure of azurin from Alcaligenes denitrificans refinement at 1·8 Å resolution and comparison of the two crystallographically independent moleculesJournal of Molecular Biology, 1988
- Kinetic studies of the copper nitrite reductase from Achromobacter cycloclastes and its interaction with a blue copper proteinBiochemical and Biophysical Research Communications, 1987
- Crystal structure analyses of reduced (CuI) poplar plastocyanin at six pH valuesJournal of Molecular Biology, 1986
- Kinetic Studies on 1:1 Electron-Transfer Reactions Involving Blue Copper Proteins. 1. Evidence for an Unreactive Form of the Reduced Protein (pH<5) and for Protein-Complex Association in Reactions of Parsley (and Spinach) PlastocyaninJournal of the American Chemical Society, 1978