Literature DB >> 210807

The electric potential field around cytochrome c and the effect of ionic strength on reaction rates of horse cytochrome c.

W H Koppenol, C A Vroonland, R Braams.   

Abstract

1. The electric potential fields around tuna ferri- and ferrocytochrome c were calculated assuming that (i) all of the lysines and arginines are protonated, (ii) all of the glutamic and aspartic acids and the terminal carboxylic acid are dissociated, and (iii) the haem has a net charge of +1e in the oxidized form. 2. Near the haem crevice high values for the potential (greater than +2.5 kT/e) are found. Consequently, electron transfer via the haem edge is favored if the oxidant or reductant is negatively charged. 3. The inhomogeneous distribution of charges leads to a dipole moment of 244 and 238 debye for oxidized and reduced tuna cytochrome c, respectively. Horse cytochrome c has dipole moments of 303 (oxidized) and 286 (reduced) debye. 4. A line through the positive and negative charge centres, the dipole axis, crosses the tuna cytochrome c surface at Ala 83 (positive part) and Lys 99 (negative part). The direction of the dipole axis of horse cytochrome c is very similar. Since the centre of the domain on the cytochrome c surface, which is involved in the binding to cytochrome c oxidase, is found at the beta-carbon of the Phe 82 in horse cytochrome c (Ferguson-Miller, S., Brautigan, D.L. and Margoliash, E. (1978) J. Biol. Chem. 253, 149--159) it is suggested that the direction of the dipole is of physiological importance. 5. The activity coefficients of horse ferri- and ferrocytochrome c were calculated as a function of ionic strength using a formula derived by Kirkwood (Kirkwood, J.G. (1934) J. Chem. Phys. 2, 351--361). 6. Due to the high net charge at pH 7.5 the influence of the dipole moments of horse ferri- and ferrocytochrome c on the respective activity coefficients can be neglected at I less than or equal to 50 mM. 7. Using the Brønsted relation the effect of ionic strength on reaction rates of horse cytochrome c was calculated. Good agreement is found between theory and experimental results reported in the literature.

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Year:  1978        PMID: 210807     DOI: 10.1016/0005-2728(78)90149-4

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  13 in total

1.  Ionic-strength-dependence of the oxidation of native and pyridoxal 5'-phosphate-modified cytochromes c by cytochrome c oxidase.

Authors:  G Kossekova; B Atanasov; R Bolli; A Azzi
Journal:  Biochem J       Date:  1989-09-01       Impact factor: 3.857

2.  Definition of cytochrome c binding domains by chemical modification: kinetics of reaction with beef mitochondrial reductase and functional organization of the respiratory chain.

Authors:  S H Speck; S Ferguson-Miller; N Osheroff; E Margoliash
Journal:  Proc Natl Acad Sci U S A       Date:  1979-01       Impact factor: 11.205

3.  Inhibiting the mitochondrial fission machinery does not prevent Bax/Bak-dependent apoptosis.

Authors:  Philippe A Parone; Dominic I James; Sandrine Da Cruz; Yves Mattenberger; Olivier Donzé; François Barja; Jean-Claude Martinou
Journal:  Mol Cell Biol       Date:  2006-10       Impact factor: 4.272

4.  Magic angle spinning 31P NMR spectroscopy reveals two essentially identical ionization states for the cardiolipin phosphates in phospholipid liposomes.

Authors:  E E Kooijman; L A Swim; Z T Graber; Y Y Tyurina; H Bayır; V E Kagan
Journal:  Biochim Biophys Acta Biomembr       Date:  2016-10-27       Impact factor: 3.747

5.  Effect of a molecular dipole on the ionic strength dependence of a biomolecular rate constant. Identification of the site of reaction.

Authors:  W H Koppenol
Journal:  Biophys J       Date:  1980-03       Impact factor: 4.033

6.  Design and engineering of a man-made diffusive electron-transport protein.

Authors:  Bryan A Fry; Lee A Solomon; P Leslie Dutton; Christopher C Moser
Journal:  Biochim Biophys Acta       Date:  2015-09-28

7.  Mapping of anion binding sites on cytochrome c by differential chemical modification of lysine residues.

Authors:  N Osheroff; D L Brautigan; E Margoliash
Journal:  Proc Natl Acad Sci U S A       Date:  1980-08       Impact factor: 11.205

8.  ATP binding to cytochrome c diminishes electron flow in the mitochondrial respiratory pathway.

Authors:  D B Craig; C J Wallace
Journal:  Protein Sci       Date:  1993-06       Impact factor: 6.725

9.  Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice.

Authors:  Naotada Ishihara; Masatoshi Nomura; Akihiro Jofuku; Hiroki Kato; Satoshi O Suzuki; Keiji Masuda; Hidenori Otera; Yae Nakanishi; Ikuya Nonaka; Yu-Ichi Goto; Naoko Taguchi; Hidetaka Morinaga; Maki Maeda; Ryoichi Takayanagi; Sadaki Yokota; Katsuyoshi Mihara
Journal:  Nat Cell Biol       Date:  2009-07-05       Impact factor: 28.824

10.  Kinetic studies on the reduction of cytochrome c. Reaction with dihydroxy conjugated compounds (catechols and quinols).

Authors:  M M Saleem; M T Wilson
Journal:  Biochem J       Date:  1982-03-01       Impact factor: 3.857

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