Results 1 to 10 of about 25,921 (203)

Cytochrome b of Isolated Chloroplasts [PDF]

European Journal of Biochemistry, 1970
1 Cytochrome composition and light-induced absorbance changes of cytochromes b and f in isolated chloroplasts have been measured in the α-band region utilizing dual-wavelength spectrophotometry. Three cytochromes appeared in reduced minus oxidized spectra, whereas only two of them, namely, cytochrome f and a cytochrome b appeared in light-induced ...
Mordhay Avron, Gozal Ben Hayyim
openaire   +3 more sources

Multi-heme Cytochromes in Shewanella oneidensis MR-1:Structures, functions and opportunities [PDF]

, 2015
Multi-heme cytochromes are employed by a range of microorganisms to transport electrons over distances of up to tens of nanometers. Perhaps the most spectacular utilization of these proteins is in the reduction of extracellular solid substrates ...
Brown JP, Collins MJ, Coursolle D, Fonseca BM, Jochen Blumberger, Julea N. Butt, Kevin M. Rosso, Marian Breuer, Song Y, Teixeira M   +9 more
core   +1 more source

The ‘porin-cytochrome’ model for microbe-to-mineral electron transfer [PDF]

, 2012
Many species of bacteria can couple anaerobic growth to the respiratory reduction of insoluble minerals containing Fe(III) or Mn(III/IV). It has been suggested that in Shewanella species electrons cross the outer membrane to extracellular substrates via ‘
Afkar, Baron, Bouhenni, Burns, Cao, Clarke, Clarke, Clarke, Coursolle, DiChristina, Dohnalkova, Donald, Eggleston, El-Naggar, Firer-Sherwood, Firer-Sherwood, Gorby, Gralnick, Hartshorne, Hartshorne, Heidelberg, Jensen, Jiang, Jiao, Johs, Kerisit, Leang, Lies, Liu, Lower, Lower, Lower, Malvankar, Malvankar, Marsili, McLean, Meitl, Myers, Peretyazhko, Pessanha, Qian, Reardon, Reguera, Reguera, Roessler, Ross, Schuetz, Shi, Shi, Smith, Strycharz-Glaven, Strycharz-Glaven, Taylor, von Canstein, Xiong, Zargar, Zhang, Zhang   +57 more
core   +2 more sources

Mechanisms of Bacterial Extracellular Electron Exchange. [PDF]

, 2016
The biochemical mechanisms by which microbes interact with extracellular soluble metal ions and insoluble redox-active minerals have been the focus of intense research over the last three decades. The process presents two challenges to the microorganism;
Butt, Julea N., Clarke, Thomas A., Edwards, Marcus J., Gomez-Perez, Laura, Richardson, David J., White, Gaye F.   +5 more
core   +1 more source

A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding [PDF]

, 2007
In bacterial c-type cytochromes, the haem cofactor is covalently attached via two cysteine residues organized in a haem c-binding motif. Here, a novel octa-haem c protein, MccA, is described that contains only seven conventional haem c-binding motifs ...
Allen J.W.A., Allen J.W.A., Allen J.W.A., Allen J.W.A., Beliaev A.S., de Vitry C., Dobbin P.S., Hartshorne S., Kroger A., Lorenzen J.P., Mileni M., Moore G.R., Mowat C.G., Scott R.A., Thony-Meyer L., Walker F.A., Wood P.M., Yang F.   +17 more
core   +1 more source

Functional and Biogenetical Heterogeneity of the Inner Membrane of Rat-Liver Mitochondria [PDF]

, 1971
Rat liver mitochondria were fragmented by a combined technique of swelling, shrinking, and sonication. Fragments of inner membrane were separated by density gradient centrifugation.
Allmann D. W., Ashwell M., Beattie D. S., Beattie D. S., Brunner G., Burstone M. S., Davis K. A., Delbruck A., Fiske C. H., Folch J., Gear A. R. L., Gear A. R. L., Gear A. R. L., Gelder B. F., Gotterer G. S., Hasegawa E., Hawley E. S., Johnson A. B., Klingenberg M., Kuntzel H., Labbe R. F., Lentz P. E., Neupert W., Neupert W., Novikoff A. B., Ohnishi K., Omura T., Parsons D. F., Parsons D. F., Pette D., Pollak J. K., Pullmann M. E., Raw J., Raw J., Reith A., Schneider W. C., Schuel H., Schumacher H.-H., Sebald W., Sebald W., Seligman A. M., Sies H., Sottocasa G. L., Stoffel W., Strecker H. J., Swick R. W., Szarkowska L., Tabor C. W., Tol A., Vazquez J. J., Yonetani T.   +50 more
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The Crystal Structure of the Extracellular 11-heme Cytochrome UndA Reveals a Conserved 10-heme Motif and Defined Binding Site for Soluble Iron Chelates [PDF]

, 2012
Members of the genus Shewanella translocate deca- or undeca-heme cytochromes to the external cell surface thus enabling respiration using extracellular minerals and polynuclear Fe(III) chelates.
Butt, Julea N., Clarke, Thomas A., Edwards, Marcus J., Fredrickson, James K., Hall, Andrea, Richardson, David J., Shi, Liang, Zachara, John M.   +7 more
core   +2 more sources

Redox linked flavin sites in extracellular decaheme proteins involved in microbe-mineral electron transfer [PDF]

, 2015
Extracellular microbe-mineral electron transfer is a major driving force for the oxidation of organic carbon in many subsurface environments. Extracellular multi-heme cytochromes of the Shewenella genus play a major role in this process but the mechanism
A Okamoto, AC Mitchell, AGW Leslie, AM Waterhouse, AS Beliaev, CL Reardon, D Coursolle, D Ghosal, DE Ross, DJ Richardson, DJ Richardson, DJ Richardson, DK Thompson, E Marsili, ED Brutinel, F Sievers, GF White, GM Boratyn, GN Murshudov, I Letunic, JK Fredrickson, L Shi, L Shi, MJ Daly, MJ Daly, MJ Edwards, MJ Edwards, MJ Edwards, MY El-Naggar, P Taylor, PD Adams, RJ Morris, RS Hartshorne, S Bailey, S Pirbadian, TA Clarke   +35 more
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The Rieske/cytochrome b complex of Heliobacteria

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2008
Heliobacteria have a Rieske/cytochrome b complex composed of a Rieske protein, a cytochrome b(6,) a subunit IV and a di-heme cytochrome c. The overall structure of the complex seems close to the b(6)f complex from cyanobacteria and chloroplasts to the exception of the di-heme cytochrome. We show here by biochemical and biophysical studies that a heme c(
Anne-Lise Ducluzeau, Line Capowiez, Frauke Baymann, E. Chenu   +3 more
openaire   +3 more sources

Biogenesis of mitochondrial c-type cytochromes [PDF]

, 1990
Cytochromesc andc 1 are essential components of the mitochondrial respiratory chain. In both cytochromes the heme group is covalently linked to the polypeptide chain via thioether bridges. The location of the two cytochromes is in the intermembrane space;
Gonzales, Daniel H., Neupert, Walter
core   +1 more source