The aim of this review is to analyze the current state of knowledge concerning the blue
copper protein plastocyanin (PC) focusing on its interactions with its reaction partners …

Cytochromes c are haemoproteins which carry out electron transfer in a wide variety of
biological systems, necessitating different kinds of cytochrome c to fulfill different biological …

The relationship between structure and function in the evolutionary-conservative cytochrome
c family has remained fragmentary and confused despite a great deal of information …

The structure of poplar plastocyanin in the reduced (Cu I) state has been determined and
refined, using counter data recorded from crystals at pH 3.8, 4.4, 5.1, 5.9, 7.0 and 7.8 …

The electron‐transfer reactions of site‐specific mutants of the blue copper protein azurin
from Pseudomonas aeruginosa with its presumed physiological redox partners cytochrome …

The rates for the photoinduced bimolecular reactions of a homologous series of RuII
diimines with cytochrome (cyt) c in its oxidized and reduced forms have been measured. The …

Mutant plastocyanins with Leu at position 10, 90 or 83 (Gly, Ala and Tyr respectively in
wildtype) were constructed by site‐specific mutagenesis of the spinach gene, and expressed …

To understand the specificity and efficiency of protein-protein interactions promoting electron
transfer, we evaluated the role of electrostatic forces in precollision orientation by the …

The electronic structure and spectrum of several models of the binuclear metal site in
soluble CuA domains of cytochrome-c oxidase have been calculated by the use of an …

Modification of the three carboxyl groups on adrenodoxin using a water-soluble
carbodiimide (1-ethyl-3-(3-dimethylaminopropyl) carbodiimide) caused a weakening of the …