A simple method for the determination of reduction potentials in heme proteins

被引:45
作者
Efimov, Igor [1 ]
Parkin, Gary [1 ]
Millett, Elizabeth S. [1 ]
Glenday, Jennifer [1 ]
Chan, Cheuk K. [1 ]
Weedon, Holly [1 ]
Randhawa, Harpreet [1 ]
Basran, Jaswir [2 ]
Raven, Emma L. [1 ]
机构
[1] Univ Leicester, Dept Chem, Leicester LE1 7RH, Leics, England
[2] Univ Leicester, Dept Biochem, Leicester LE1 9HN, Leics, England
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
Heme; Heme protein; Reduction potential; Redox; HUMAN INDOLEAMINE 2,3-DIOXYGENASE; HEART CYTOCHROME-C; ACTIVE-SITE; SPECTROSCOPIC CHARACTERIZATION; ELECTROCATALYTIC PROPERTIES; TRYPTOPHAN 2,3-DIOXYGENASE; ASCORBATE PEROXIDASE; CATALYTIC-PROPERTIES; CIRCADIAN-RHYTHMS; ELECTRON-TRANSFER;
D O I
10.1016/j.febslet.2013.12.030
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We describe a simple method for the determination of heme protein reduction potentials. We use the method to determine the reduction potentials for the PAS-A domains of the regulatory heme proteins human NPAS2 (E-m = 115 mV +/- 2 mV, pH 7.0) and human CLOCK (E-m = 111 mV +/- 2 mV, pH 7.0). We suggest that the method can be easily and routinely applied to the determination of reduction potentials across the family of heme proteins. (C) 2014 The Authors. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:701 / 704
页数:4
相关论文
共 48 条
[1]   A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase [J].
Basran, Jaswir ;
Rafice, Sara A. ;
Chauhan, Nishma ;
Efimov, Igor ;
Cheesman, Myles R. ;
Ghamsari, Lila ;
Raven, Emma Lloyd .
BIOCHEMISTRY, 2008, 47 (16) :4752-4760
[2]   Control of cytochrome c redox potential:: Axial ligation and protein environment effects [J].
Battistuzzi, G ;
Borsari, M ;
Cowan, JA ;
Ranieri, A ;
Sola, M .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (19) :5315-5324
[3]   Redox properties of heme peroxidases [J].
Battistuzzi, Gianantonio ;
Bellei, Marzia ;
Bortolotti, Carlo Augusto ;
Sola, Marco .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2010, 500 (01) :21-36
[4]   The birth of protein electrochemistry [J].
Blanford, Christopher F. .
CHEMICAL COMMUNICATIONS, 2013, 49 (95) :11130-11132
[5]   The Reversible Opening of Water Channels in Cytochrome c Modulates the Heme Iron Reduction Potential [J].
Bortolotti, Carlo Augusto ;
Amadei, Andrea ;
Aschi, Massimiliano ;
Borsari, Marco ;
Corni, Stefano ;
Sola, Marco ;
Daidone, Isabella .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2012, 134 (33) :13670-13678
[6]   CYCLIC VOLTAMMETRY AND DERIVATIVE CYCLIC VOLTABSORPTOMETRY OF PURIFIED HORSE HEART CYTOCHROME-C AT TIN-DOPED INDIUM OXIDE OPTICALLY TRANSPARENT ELECTRODES [J].
BOWDEN, EF ;
HAWKRIDGE, FM ;
CHLEBOWSKI, JF ;
BANCROFT, EE ;
THORPE, C ;
BLOUNT, HN .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1982, 104 (26) :7641-7644
[7]   Electron transfer and electrocatalytic properties of the immobilized Methionine80Alanine cytochrome c variant [J].
Casalini, Stefano ;
Battistuzzi, Gianantonio ;
Borsari, Marco ;
Bortolotti, Carlo Augusto ;
Ranieri, Antonio ;
Sola, Marco .
JOURNAL OF PHYSICAL CHEMISTRY B, 2008, 112 (05) :1555-1563
[8]   The role of serine 167 in human indoleamine 2,3-dioxygenase: A comparison with tryptophan 2,3-dioxygenase [J].
Chauhan, Nishma ;
Basran, Jaswir ;
Efimov, Igor ;
Svistunenko, Dimitri A. ;
Seward, Harriet E. ;
Moody, Peter C. E. ;
Raven, Emma Lloyd .
BIOCHEMISTRY, 2008, 47 (16) :4761-4769
[9]  
Clark W.M., 1960, OXIDATION REDUCTION
[10]   ROLE OF ARGININE-38 IN REGULATION OF THE CYTOCHROME-C OXIDATION-REDUCTION EQUILIBRIUM [J].
CUTLER, RL ;
DAVIES, AM ;
CREIGHTON, S ;
WARSHEL, A ;
MOORE, GR ;
SMITH, M ;
MAUK, AG .
BIOCHEMISTRY, 1989, 28 (08) :3188-3197