1997
DOI: 10.1021/jp962478o
|View full text |Cite
|
Sign up to set email alerts
|

The Reorganization Energy of Cytochrome c Revisited

Abstract: The solution structures of the reduced and oxidized forms of the cytochrome c are used to reevaluate the reorganization energy for oxidation of cytochrome c. This is achieved by using the linear response approximation in concert with the NMR structures as pseudo energy constraints. Alternative estimates, obtained using a free energy perturbation approach employing umbrella sampling and a continuum dielectric approach, are also provided. The reorganization energy obtained is larger than that previously estimate… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

32
289
3
2

Year Published

1998
1998
2009
2009

Publication Types

Select...
9

Relationship

3
6

Authors

Journals

citations
Cited by 226 publications
(326 citation statements)
references
References 59 publications
32
289
3
2
Order By: Relevance
“…35. The distribution of titratable residues for our model of CcO is close to that for the "ionized" protein model 47 of cytochrome c for which the estimation p = 2.9 remarkably correlates with our result.…”
Section: Conclusion and Discussionsupporting
confidence: 86%
See 1 more Smart Citation
“…35. The distribution of titratable residues for our model of CcO is close to that for the "ionized" protein model 47 of cytochrome c for which the estimation p = 2.9 remarkably correlates with our result.…”
Section: Conclusion and Discussionsupporting
confidence: 86%
“…Indeed, matching ⌬G MD rf to the continuum free energy yields p = 1.3 for the dry CcO ͑see above subsection͒, which is unphysically low for the static dielectric constant for a condensed phase; indeed, it is even lower than pure electronic polarizability el ϳ 2. In contrast, MDEC approach leads to physically reasonable estimations that are in line with results of other authors 47 ͑see Sec. IV͒.…”
Section: Standard Continuum Modelsupporting
confidence: 91%
“…c the heme group is surrounded by a hydrophobic and relatively rigid pocket (12,13), and the protein contribution to the reorganization energy of cyt. c is thought to be weak (14,15). Structural flexibility is not advantageous for that function.…”
mentioning
confidence: 99%
“…For example, sixcoordinate bis-His-hemes have E m s ranging from -410 to +360 mV with the redox differences being predominately due to the intraprotein electrostatic environment (1,(20)(21)(22). In these proteins the loss of solvation energy (15,23,24), interactions with the protein backbone and with other residues (15,(20)(21)(22)25), and local conformation changes on ionization changes (20,26) determine the thermodynamic equilibrium measured by pK a s and E m s.…”
mentioning
confidence: 99%