Cupredoxins—A study of how proteins may evolve to use metals for bioenergetic processes

Molecular Modeling of the Ternary Complex of Rusticyanin-Cytochrome c4-Cytochrome Oxidase: An Insight to Possible H-Bond Mediated Recognition and Electron Transfer Reaction inT.ferrooxidans

(2012) B. P. Mukhopadhyay et al.   JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS

Surface residues dynamically organize water bridges to enhance electron transfer between proteins

(2010) A. de la Lande et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Defining the Role of the Axial Ligand of the Type 1 Copper Site in Amicyanin by Replacement of Methionine with Leucine

(2009) Moonsung Choi et al.   BIOCHEMISTRY

Rationally tuning the reduction potential of a single cupredoxin beyond the natural range

(2009) Nicholas M. Marshall et al.   NATURE

Protein Control of True, Gated, and Coupled Electron Transfer Reactions

(2008) Victor L. Davidson   ACCOUNTS OF CHEMICAL RESEARCH

The axial ligand and extent of protein folding determine whether Zn or Cu binds to amicyanin

(2007) John K. Ma et al.   JOURNAL OF INORGANIC BIOCHEMISTRY