Results 21 to 30 of about 885 (161)

Efficient and selective isotopic labeling of hemes to facilitate the study of multiheme proteins

BioTechniques, 2012
Specific isotopic labeling of hemes provides a unique opportunity to characterize the structure and function of heme-proteins. Unfortunately, current methods do not allow efficient labeling in high yields of multiheme cytochromes c, which are of great ...
Bruno M. Fonseca, Ming Tien, Mario Rivera, Liang Shi, Ricardo O. Louro   +4 more
doaj   +1 more source

The role of intramolecular interactions in the functional control of multiheme cytochromes c [PDF]

FEBS Letters, 2011
Detailed thermodynamic and structural data measured in soluble monomeric multiheme cytochromes c provided the basis to investigate the functional significance of interactions between redox co‐factors. The steep decay of intramolecular interactions with distance means that close proximity of the redox centers is necessary to modulate the intrinsic ...
Fonseca, Bruno M., Paquete, Catarina M., Salgueiro, Carlos A., Louro, Ricardo O.   +3 more
openaire   +2 more sources

Abundance of the multiheme c-type cytochrome OmcB increases in outer biofilm layers of electrode-grown Geobacter sulfurreducens. [PDF]

PLoS ONE, 2014
When Geobacter sulfurreducens utilizes an electrode as its electron acceptor, cells embed themselves in a conductive biofilm tens of microns thick.
Camille S Stephen, Edward V LaBelle, Susan L Brantley, Daniel R Bond   +3 more
doaj   +1 more source

Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family [PDF]

, 2012
Shewanella oneidensis MR-1 has the ability to use many external terminal electron acceptors during anaerobic respiration, such as DMSO. The pathway that facilitates this electron transfer includes the decahaem cytochrome DmsE, a paralogue of the MtrA ...
Altschul, Beliaev, Bilous, Bucking, Cammack, Catherine L. Drennan, Clarke, Clarke, Coursolle, Coursolle, Dohnalkova, Firer-Sherwood, Firer-Sherwood, Firer-Sherwood, Gao, Gao, Gralnick, Gralnick, Hartshorne, Hartshorne, Jee-Young Mock, Jiao, Kathryn D. Bewley, Liu, Lovley, Lovley, Mackenzie A. Firer-Sherwood, Matias, McMillan, Myers, Myers, Myers, Myers, Myers, Nealson, Nozomi Ando, Pitts, Ross, Schuetz, Schwalb, Sean J. Elliott, Shannon, Sharma, Shi, Shi, Zhang   +45 more
core   +1 more source

Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1

Frontiers in Microbiology, 2015
The versatile anaerobic metabolism of the Gram-negative bacterium Shewanella oneidensis MR-1 (SOMR-1) relies on a multitude of redox proteins found in its periplasm.
Mónica N. Alves, Sónia E. Neto, Alexandra S. Alves, Afonso eCarrêlo, Isabel ePacheco, Bruno M. Fonseca, Catarina M. Paquete, Cláudio M. Soares, Ricardo O Louro   +8 more
doaj   +1 more source

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

Molecular Mechanisms of Microbial Extracellular Electron Transfer: The Importance of Multiheme Cytochromes

Frontiers in Bioscience-Landmark, 2022
Extracellular electron transfer is a key metabolic process of many organisms that enables them to exchange electrons with extracellular electron donors/acceptors. The discovery of organisms with these abilities and the understanding of their electron transfer processes has become a priority for the scientific and industrial community, given the growing
Catarina M. Paquete, Leonor Morgado, Carlos A. Salgueiro, Ricardo O. Louro   +3 more
openaire   +3 more sources

The Ion-Translocating NrfD-Like Subunit of Energy-Transducing Membrane Complexes

Frontiers in Chemistry, 2021
Several energy-transducing microbial enzymes have their peripheral subunits connected to the membrane through an integral membrane protein, that interacts with quinones but does not have redox cofactors, the so-called NrfD-like subunit.
Filipa Calisto, Filipa Calisto, Manuela M. Pereira, Manuela M. Pereira   +3 more
doaj   +1 more source

Multiheme Cytochromes from the Sulfur‐Reducing Bacterium Desulfuromonas Acetoxidans [PDF]

European Journal of Biochemistry, 1997
Two new multiheme cytochromes were isolated from the anaerobic sulfur reducing bacterium Desulfuromonas acetoxidans. They have monomeric molecular masses of 50 and 65 kDa and contain six and eight hemes, respectively. Visible and EPR spectroscopies, in the as‐isolated (oxidised) cytochromes, show the presence of only low‐spin hemes in the 50‐kDa ...
I A, Pereira, I, Pacheco, M Y, Liu, J, Legall, A V, Xavier, M, Teixeira   +5 more
openaire   +2 more sources

How Thermophilic Gram-Positive Organisms Perform Extracellular Electron Transfer: Characterization of the Cell Surface Terminal Reductase OcwA

mBio, 2019
Extracellular electron transfer is the key process underpinning the development of bioelectrochemical systems for the production of energy or added-value compounds.
N. L. Costa, B. Hermann, V. Fourmond, M. M. Faustino, M. Teixeira, O. Einsle, C. M. Paquete, R. O. Louro   +7 more
doaj   +1 more source