Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible
structure, particularly in the ferric form, such that it is able to sample a broad conformational …

1. History 3422. Activation barriers 3432.1 Redox potentials 3442.2 Reorganization energy
3443. Electronic coupling 3454. Ru-modified proteins 3484.1 Reorganization energy …

The ability of metalloproteins to recognize their biological redox partners, as well as kinetics
of inter-protein electron-transfer reactions may be affected by chemical modification of amino …

Axial iron ligation and protein encapsulation of the heme cofactor have been investigated as
effectors of the reduction potential (E°') of cytochrome c through direct electrochemistry …

The redox behavior of cytochrome c (cyt c) adsorbed to gold electrodes modified with self-
assembled monolayers (SAMs) depends on the SAM. This paper examines SAMs …

c proteins of known sequence have been modeled in the oxidized state based on the
existing crystallographic and NMR structures. The secondary structural elements and the …

Splitting the reduction potential of electron transport (ET) proteins and redox
metalloenzymes into the enthalpic and entropic contributions is an insightful practice to …

Oxidation of cardiolipin (CL) by its complex with cytochrome c (cyt c) plays a crucial role in
triggering apoptosis. Through a combination of magnetic circular dichroism spectroscopy …

The thermodynamic parameters of protein reduction (Δ H°'rc and ΔS°'rc) were measured for
a number of blue copper proteins including spinach plastocyanin, cucumber plastocyanin …

A new dye-decolorizing peroxidase (DyP) was discovered through a data mining workflow
based on HMMER software and profile Hidden Markov Model (HMM) using a dataset of …