Electron transfer in biology. The function of cytochrome c

Moore, Geoffrey R.; Huang, Zhong‐Xian; Eley, Crispin G. S.; Barker, Hazel A.; Williams, G. D.; Robinson, Martin N.; Williams, R. J. P.

doi:10.1039/dc9827400311

Cited by 55 publications

(19 citation statements)

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“…2 we plot the theoretical paramagnetic shift expected from the crystal structure and calculated from the theory of the rhombic paramagnetic shift (see [20,21]) against the observed paramagnetic shift. The observations led not only to the general result that the structures in solution and crystal were closely similar but enabled us to see points of difference and to define the dynamics over a wide temperature range [22,23]. Examples of ring current shifts will be analysed later in the article 1241.…”

Section: Frequency Shiftsmentioning

confidence: 90%

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NMR studies of mobility within protein structure

Williams

1989

European Journal of Biochemistry

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NMR studies of dynamics within structure have revealed that a quite new approach to protein structure and its relation to function is necessary. This approach requires the consideration in detail of the following :1. Local movements of groups and small segments to allow fast recognition and fitting. The motion concerns on/off rates as well as binding. The observations affect surface/surface recognition, e.g. of antigen/antibody as well as of substrate and protein.2. Somewhat larger interdomain or N-and C-terminal segments which allow rearrangement. Cases in point are the movement of segments in blood-clotting proteins or in histones.3. Relative motion of helices in hinges. These actions are likely in such enzymes as kinases and P-450 cytochromes.4. Relative motion of helices within domains (relative to other helices or sheets) in mechanical devices (triggers) e.g. in cdlmodulin.5. General motion in random proteins. Examples extend from rubber-like proteins (entropy sensors), some glycoproteins, to proteins carrying peptide hormones to be generated only after hydrolysis.6. Order -+ disorder transitions locally as in osteocalcin and metallothionine. 7. Swinging arm motions associated with special sequences such as (Ala-Pro),. 8. Of great interest is the power of NMR to look at proteins which are relatively large, up to 50 k Da proteins, and to isolate certain zones of interest. This needs careful temperature dependent studies and analysis of separated domains [72] as well as the use of a great variety of pulse sequences [15] and of nuclei other than protons.9. In this article 1 have illustrated the different possibilities using work in my own group. This is done to lessen the burden of extensive review. I fully realise that the range of examples is now large. I would stress though that the production of the necessary technology was the endeavour of several of us within the Oxford Enzyme Group from 1970 to 1985, i.e. from 270-600 MHz Fourier-transform NMR spectroscopy.10. While all of these features have been demonstrated by NMR methods there are parallel developments both using X-ray diffraction methods and theoretical approaches. All these procedures are changing the view of protein structure to one which incorporates dynamics all the way from conventional vibronic/rotational coupling to the disordered motions characteristic of random polymers. It is the understanding of dynamics that leads to an appreciation of function.Correspondence ta R. J. P. Williams, Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QR, EnglandAbbreviations. FUR protein, iron-uptake regulatory protein; NOE, nuclear Overhauser effect; COSY, correlated spectroscopy; NOESY, nuclear Overhauser effect spectroscopy; Gla, y-carboxyglutamate.No&. While this article was being completed, a review was published in the European Journal of Biochemistry [76] which has summarised very effectively some of the problems faced by all users of NMR methods who attempt to describe either structure or dynamics of large flexible...

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Section: Frequency Shiftsmentioning

confidence: 90%

“…This is a slow reaction. (b) The temperature of the low-spin to high-spin switch, which is just a breaking of the Met80 -Fe bond [23]. The switch is in fast exchange.…”

Section: Groove Opening [53 541mentioning

confidence: 99%

NMR studies of mobility within protein structure

Williams

1989

European Journal of Biochemistry

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“…A search for the biochemical rational behind the persistent occurrence of histidine and methionine as axial ligands of the haem-iron has been our motivation for systematic studies of correlations between the active site conformation and the primary structure, the electronic structure of haem c and functional properties, such as the redox potential or the reactivity with cytochrome oxidases and reductases from different species. The omnipresence of soluble c-type cytochromes in nature has already stimulated many comparative structural (Dickerson & Timkovitch, 1975;Timkovitch, 1979;Moore et al 1982), evolutionary (Meyer & Kamen, 1982;Dickerson, 19800,6,c) and functional studies (Ferguson-Miller et al 1979;Errede & Kamen, 1978;Yamanaka & Okunuki, 1968;Sutin, 1977). Thereby the characterization of the protein surface responsible for the interaction with physiological redox-partners has been the target of numerous recent biochemical investigations (Ferguson-Miller et al 1979;Rieder & Bosshard, 1980;Waldmeyer et al 1982;Kraut, 1981).…”

Section: P H Y L O G E N E S I S Of H a E M -I R O N C O -O R D I N Amentioning

confidence: 99%

“…The apparent free energy of electron transfer would be lowered as a result of this conformation change. Experimental support for the potential of c-type cytochromes to adopt such intermediate structures comes from single crystal X-ray studies (Takano & Dickerson, 19810,6;Matsuura et al 1982), chemical modification (Ferguson-Miller et al 1979;Osheroff et al 1979Osheroff et al , 1980Koppenol & Margoliash, 1982) and NMR studies (Moore et al 1982;Senn et al 1983 a, 19846;Keller & Wiithrich, 1981). These studies also show that the biologically interacting surface of the globular molecule lies close to the axial methionine and is conformationally rather flexible.…”

Section: Correlation Between the Co-ordination Geometry Of The Axial mentioning

confidence: 99%

“…Experimental support for this hypothesis comes from enzymatic studies with various primate cytochromes c where a correlation has been found between productive complex formation and transition properties of the axial methionine sensitive absorption band at 695 nm (Osheroff et al 1979). Further, the above hypothesis on the fine control of cytochrome c function are also based on the observation that the cytochrome c molecular structure is more flexible on the methionine side of the haem c (Keller & Wuthrich, 1981;Moore & Williams, 1980;Moore et al 1982;Senn et al 1983a, 19846;Takano & Dickerson 19816). …”

Section: (C) Axial Methionine Co-ordination and Enzymatic Activitymentioning

confidence: 99%

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Amino acid sequence, haem-iron co-ordination geometry and functional properties of mitochondrial and bacterial c-type cytochromes

Senn

Wüthrich

1985

Quart. Rev. Biophys.

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Cytochromes are found in all biological oxidation Systems which involve transport of reducing equivalents through organized chains of membrane bound intermediates, regardless of the ultimate oxidant (Keilin, 1966; Bartsch, 1978; Meyer & Kamen, 1982). Thus, cytochromes are present not only in the aerobic mitochondrial and bac-terial respiratory chain, but are also found in much more diversified procariotic Systems, including all varieties of facultative anaerobes (nitrate and nitrite reducers), obligate anaerobes (sulphate reducers and phototrophic sulphur bacteria), facultative photoheterotrophes (phototrophic non-sulphur purple bacteria), and the photoautotrophic cyanobacteria (blue-green algae). Among the different types of cytochromes occurring in the cell, the soluble c-type cytochromes (‘class I’, Meyer & Kamen, 1982) are the most abundant and best characterized group of proteins (Bartsch, 1978; Meyer & Kamen, 1982; Dickerson & Timkovitch, 1975; Lemberg & Barrett, 1973; Salemme, 1977; Ferguson-Miller, Brautigan & Margoliash, 1979). The amino acid sequences of more than 80 mitochrondrial and close to 40 bacterial cytochromes c are known (Meyer & Kamen, 1982; Dickerson & Timkovitch, 1975; Schwartz & Dayhoff, 1976; Dayhoff & Barker, 1978).

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Functionalization of gold electrode surface with heterobifunctional poly(ethylene oxide)s having both mercapto and aldehyde groups

Kurusu¹,

Ohno²,

Kaneko³

et al. 2003

Polymers for Advanced Techs

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We synthesized heterobifunctional poly(ethylene oxide) (PEO) (α‐formyl‐ω‐mercapto‐PEO; CHO‐PEO400‐SH, average molecular weight of PEO part being 400), which had both an aldehyde group as a binding site with amino group of protein and a mercapto group for gold electrode surface. The CHO‐PEO400‐SH was adsorbed on a gold electrode surface and cytochrome c (cyt.c) was fixed on this modified electrode. The redox response of covalently immobilized cyt.c was observed on the cyclic voltammetry measurement, showing that CHO‐PEO400‐SH can be used as a linker to fix cyt.c on an electrode. Another type of heterobifunctional PEO (α‐formyl‐ω‐(2‐pyridyldithio)‐PEO; CHO‐PEO300‐SS‐Py), which had an aldehyde group and a 2‐pyridinethiol (2‐Py) through disulfide bond, was synthesized to form co‐adsorbed monolayer of PEO chain and 2‐Py on an electrode surface. It was expected, due to the spacer with shorter PEO chain and lower surface density, that better redox response of the fixed cyt.c was obtained. However, the redox response of fixed cyt.c was not detected on the CHO‐PEO300‐SS‐Py modified gold electrode. Instead, this heterobifunctional PEO was found to function as a good promoter for cyt.c dissolved in phosphate buffer solution. Copyright © 2003 John Wiley & Sons, Ltd.

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Electron transfer in biology. The function of cytochrome c

Cited by 55 publications

References 1 publication

NMR studies of mobility within protein structure

NMR studies of mobility within protein structure

Amino acid sequence, haem-iron co-ordination geometry and functional properties of mitochondrial and bacterial c-type cytochromes

Functionalization of gold electrode surface with heterobifunctional poly(ethylene oxide)s having both mercapto and aldehyde groups

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