Abstract We examine vibrational energy transfer across the heme–protein and protein–solvent interfaces of cyto-chrome c, using, as appropriate, classical, semiclassical, and quantum approaches. To characterize energy flow across the interface between the heme and the rest of cytochrome c, we calculate communication maps for the protein in its native structure as well as two structures with Met80 dissociated from the heme at 300 K. The response to excess energy in the heme is mediated by covalent and hydrogen bonds to the heme, as well as several through-space interactions, including those involving the dissoci-ated Met80. This observation suggests no energy flow bottleneck between the heme and Met80 that would impede rebinding kinetics at 3...
Elucidation of the molecular determinants of the reorganization energy λ is central to the understan...
Cytochrome <i>c</i> (Cyt <i>c</i>) has a heme covalently bound to the polypeptide via a Cys-X-X-Cys-...
ABSTRACT: Cytochrome c (Cyt c) has a heme covalently bound to the polypeptide via a Cys-X-X-Cys-His ...
The rate and mechanism of the kinetic energy relaxation of directly excited heme in cytochrome c was...
The active site of cytochrome c (Cyt c) consists of a heme covalently linked to a pentapeptide segme...
AbstractBy constructing a continuity equation of energy flow, one can utilize results from a molecul...
In a combined experimental–theoretical study, we investigated the transport of vibrational energy fr...
The kinetic energy relaxation of photolyzed heme in myoglobin was investigated using molecular dynam...
The folding energy landscape of cytochrome c is complicated by a large, covalently bound heme cofact...
Elucidation of the molecular determinants of the reorganization energy λ is central to the understan...
© 2014 American Chemical Society. Cytochrome c (Cyt c) has a heme covalently bound to the polypeptid...
ABSTRACT Cytochrome c oxidase mediates the final step of electron transfer reactions in the respirat...
A pathway of vibrational energy flow in myoglobin was studied by time-resolved anti-Stokes ultraviol...
AbstractCytochrome c oxidase mediates the final step of electron transfer reactions in the respirato...
ABSTRACT The vibrational energy relaxation of a selected vibrational mode in cytochrome c—a C-D stre...
Elucidation of the molecular determinants of the reorganization energy λ is central to the understan...
Cytochrome <i>c</i> (Cyt <i>c</i>) has a heme covalently bound to the polypeptide via a Cys-X-X-Cys-...
ABSTRACT: Cytochrome c (Cyt c) has a heme covalently bound to the polypeptide via a Cys-X-X-Cys-His ...
The rate and mechanism of the kinetic energy relaxation of directly excited heme in cytochrome c was...
The active site of cytochrome c (Cyt c) consists of a heme covalently linked to a pentapeptide segme...
AbstractBy constructing a continuity equation of energy flow, one can utilize results from a molecul...
In a combined experimental–theoretical study, we investigated the transport of vibrational energy fr...
The kinetic energy relaxation of photolyzed heme in myoglobin was investigated using molecular dynam...
The folding energy landscape of cytochrome c is complicated by a large, covalently bound heme cofact...
Elucidation of the molecular determinants of the reorganization energy λ is central to the understan...
© 2014 American Chemical Society. Cytochrome c (Cyt c) has a heme covalently bound to the polypeptid...
ABSTRACT Cytochrome c oxidase mediates the final step of electron transfer reactions in the respirat...
A pathway of vibrational energy flow in myoglobin was studied by time-resolved anti-Stokes ultraviol...
AbstractCytochrome c oxidase mediates the final step of electron transfer reactions in the respirato...
ABSTRACT The vibrational energy relaxation of a selected vibrational mode in cytochrome c—a C-D stre...
Elucidation of the molecular determinants of the reorganization energy λ is central to the understan...
Cytochrome <i>c</i> (Cyt <i>c</i>) has a heme covalently bound to the polypeptide via a Cys-X-X-Cys-...
ABSTRACT: Cytochrome c (Cyt c) has a heme covalently bound to the polypeptide via a Cys-X-X-Cys-His ...