pH dependence of heme electrochemistry in cytochromes investigated by multiconformation continuum electrostatic calculations

Hauser, Karin; Mao, Junjun; Gunner, Marilyn R.

pH dependence of heme electrochemistry in cytochromes investigated by multiconformation continuum electrostatic calculations

Dateien

Hauser_pH Dependence.pdfGröße: 69.51 KBDownloads: 286

Datum

2004

Autor:innen

Hauser, Karin

Mao, Junjun

Gunner, Marilyn R.

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Chemie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Biopolymers. 2004, 74(1-2), pp. 51-54. ISSN 0006-3525. Available under: doi: 10.1002/bip.20042

Zusammenfassung

Cytochromes belong to a diverse family of heme-containing redox proteins that function as intermediaries in electron transfer chains. They can be soluble, extrinsic, or intrinsic membrane proteins, and are found in different structural motifs (globin, 4-helix bundles, roll, sandwich). Measured electrochemical midpoint potentials vary over a wide range even though the basic redox reaction at the heme is the same for all cytochromes. The perturbation of the heme electrochemistry is induced by the protein structure. Also, the pH dependence varies since it depends on the strength of interaction between the heme and surrounding residues as well as the ionization states of these groups. Multiconformation continuum electrostatics (MCCE) has been used to investigate the pH dependence of heme electrochemistry in cytochromes with different folds. Often propionates are the primary contributors for pH dependence especially if they are partially protonated in the reduced heme as it is shown for globin cytochrome c551 P. aeruginosa and cytochrome b5 R. norvegicus (roll). However, if the propionates are already fully ionized at a certain pH they do not contribute to the pH dependence even if they have big interaction with the heme. At pH 7 there is no propionate contribution for cytochrome f C. reinhardtii (sandwich) and the 4-helix bundle c R. palustris. Other residues can also change their ionization significantly during heme oxidation and therefore be involved in proton release and pH dependence. These residues have been identified for different cytochrome types.

Fachgebiet (DDC)

540 Chemie

Schlagwörter

cytochrome, heme electrochemistry, pH dependence, electrostatic calculations

Zitieren

ISO 690

HAUSER, Karin, Junjun MAO, Marilyn R. GUNNER, 2004. pH dependence of heme electrochemistry in cytochromes investigated by multiconformation continuum electrostatic calculations. In: Biopolymers. 2004, 74(1-2), pp. 51-54. ISSN 0006-3525. Available under: doi: 10.1002/bip.20042

BibTex

@article{Hauser2004-05-05depen-17553,
  year={2004},
  doi={10.1002/bip.20042},
  title={pH dependence of heme electrochemistry in cytochromes investigated by multiconformation continuum electrostatic calculations},
  number={1-2},
  volume={74},
  issn={0006-3525},
  journal={Biopolymers},
  pages={51--54},
  author={Hauser, Karin and Mao, Junjun and Gunner, Marilyn R.}
}

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