Reaction pathways in the enzymatic formation and cleavage of the N-N and N-O bonds, respectively, are difficult to verify without the structure of the intermediates, but we now have such information on the heme a3 2+-NO ...

The tunneling pathway framework description of protein electron transfer reactions has prompted a lively discussion of how structure and evolution influence electron transfer rates. Recent protein and model system experiments, ...

The understanding of the dynamics and conformational control involved in the interplay between structure and function of nitric oxide reductase (Nor) and heme-copper oxidoreductases in their function to convert nitric oxide ...

The dioxygen reduction mechanism in cytochrome oxidases relies on proton control of the electron transfer events that drive the process. Proton delivery and proton channels in the protein that are relevant to substrate ...

Identification of the intermediates and determination of their structures in the reduction of dioxygen to water by cytochrome c oxidase (CcO) are particularly important to understanding both O2 activation and proton pumping ...

Resonance Raman spectroscopy has been employed to investigate the reduced cyano complexes of cytochrome aa3 from bovine heart and Rhodobacter sphaeroides and of cytochrome bo3 from E. coli. In the aa 3-type oxidases, the ...

Understanding of the chemical nature of the dioxygen and nitric oxide moiety of ba3-cytochrome c oxidase from Thermus thermophilus is crucial for elucidation of its physiological function. In the present work, direct ...

Time-resolved resonance Raman (TR3) and time-resolved step-scan (TRS2) FTIR spectroscopies have been used to probe the structural dynamics at the heme b3 proximal and distal sites after carbon monoxide photolysis from fully ...