BIOMAT Database Logo BIOMAT Database Logo

Electron transfer reactions of copper proteins. 1976

R A Holwerda, and S Wherland, and H B Gray

UI MeSH Term Description Entries
D008667 Metalloproteins Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed) Metalloprotein
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010940 Plant Proteins Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available. Plant Protein,Protein, Plant,Proteins, Plant
D010970 Plastocyanin A copper-containing plant protein that is a fundamental link in the electron transport chain of green plants during the photosynthetic conversion of light energy by photophosphorylation into the potential energy of chemical bonds. Plastocyanine,Silver Plastocyanin,Plastocyanin, Silver
D011124 Polyporaceae A family of bracket fungi, order POLYPORALES, living in decaying plant matter and timber.
D011550 Pseudomonas aeruginosa A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection. Bacillus aeruginosus,Bacillus pyocyaneus,Bacterium aeruginosum,Bacterium pyocyaneum,Micrococcus pyocyaneus,Pseudomonas polycolor,Pseudomonas pyocyanea
D011551 Pseudomonas fluorescens A species of nonpathogenic fluorescent bacteria found in feces, sewage, soil, and water, and which liquefy gelatin. Bacillus fluorescens,Bacillus fluorescens liquefaciens,Bacterium fluorescens,Liquidomonas fluorescens
D002570 Ceruloplasmin A multi-copper blood FERROXIDASE involved in iron and copper homeostasis and inflammation. Caeruloplasmin,Ferroxidase,Ceruloplasmin Ferroxidase,Ceruloplasmin Oxidase,Ferroxidase I,alpha(2)-Ceruloplasmin,Ferroxidase, Ceruloplasmin,Oxidase, Ceruloplasmin
D003300 Copper A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55. Copper-63,Copper 63
D003580 Cytochromes Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands. Cytochrome

Related Publications

R A Holwerda, and S Wherland, and H B Gray
Reactions of electron-transfer proteins at electrodes.
August 1985, Quarterly reviews of biophysics,
R A Holwerda, and S Wherland, and H B Gray
Activation of electron transfer reactions of the blue proteins.
April 1978, Biophysical journal,
R A Holwerda, and S Wherland, and H B Gray
Direct electron transfer between copper-containing proteins and electrodes.
June 2005, Biosensors & bioelectronics,
R A Holwerda, and S Wherland, and H B Gray
Investigation of electron-transfer reactions of proteins by electrochemical methods.
July 1981, Bioscience reports,
R A Holwerda, and S Wherland, and H B Gray
Protein-protein electron transfer. A Marcus theory analysis of reactions between c type cytochromes and blue copper proteins.
June 1978, Biochemistry,
R A Holwerda, and S Wherland, and H B Gray
Bacterial nitrous oxide respiration: electron transport chains and copper transfer reactions.
January 2019, Advances in microbial physiology,
R A Holwerda, and S Wherland, and H B Gray
Copper Guanidinoquinoline Complexes as Entatic State Models of Electron-Transfer Proteins.
November 2017, Chemistry (Weinheim an der Bergstrasse, Germany),
R A Holwerda, and S Wherland, and H B Gray
Preferred sites and pathways for electron transfer in blue copper proteins.
January 1988, Progress in clinical and biological research,
R A Holwerda, and S Wherland, and H B Gray
Biological electron-transfer reactions.
January 1999, Essays in biochemistry,
R A Holwerda, and S Wherland, and H B Gray
Electron transfer by copper centers.
February 2004, Chemical reviews,
Copied contents to your clipboard!