Results 131 to 140 of about 885 (161)

Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR

Chemical Communications, 2014
Residual dipolar couplings measured by NMR spectroscopy reveal that the rhombicity of the electronic structure of low-spin paramagnetic hemes determines their relative contribution to the preferential orientation of a protein with multiple hemes when placed in a strong magnetic field.
S E, Neto, B M, Fonseca, C, Maycock, R O, Louro   +3 more
openaire   +2 more sources

A systematic investigation of multiheme c-type cytochromes in prokaryotes

JBIC Journal of Biological Inorganic Chemistry, 2010
Multiheme c-type cytochromes (MHCs) are metalloproteins that can play various biochemical roles, including enzymatic activity and electron transfer. As electron transfer proteins, the presence of multiple heme cofactors in the vicinity allows electrons to rapidly travel relatively long distances.
SHARMA, SHAILESH, CAVALLARO, GABRIELE, ROSATO, ANTONIO   +2 more
openaire   +3 more sources

Structural and functional insights of GSU0105, a unique multiheme cytochrome from G. sulfurreducens

Biophysical Journal, 2021
Geobacter sulfurreducens possesses over 100 cytochromes that assure an effective electron transfer to the cell exterior. The most abundant group of cytochromes in this microorganism is the PpcA family, composed of five periplasmic triheme cytochromes with high structural homology and identical heme coordination (His-His).
Fernandes, Tomás M., Folgosa, Filipe, Teixeira, Miguel, Salgueiro, Carlos A., Morgado, Leonor   +4 more
openaire   +2 more sources

Resonance Raman fingerprinting of multiheme cytochromes from the cytochrome c 3 family

JBIC Journal of Biological Inorganic Chemistry, 2005
Resonance Raman (RR) spectroscopy was used to investigate conformational characteristics of the hemes of several ferricytochromes of the cytochrome c3 family, electron transfer proteins isolated from the periplasm and membranes of sulfate-reducing bacteria.
Roberto E, Di Paolo, Patrícia M, Pereira, Inês, Gomes, Filipa M A, Valente, Inês A C, Pereira, Ricardo, Franco   +5 more
openaire   +2 more sources

Isotopic labeling of c-type multiheme cytochromes overexpressed in E. coli

Protein Expression and Purification, 2008
Progresses made in bacterial genome sequencing show a remarkable profusion of multiheme c-type cytochromes in many bacteria, highlighting the importance of these proteins in different cellular events. However, the characterization of multiheme cytochromes has been significantly retarded by the numerous experimental challenges encountered by researchers
Ana P Fernandes, Isabel Couto, Leonor Morgado   +2 more
exaly   +3 more sources

The Production of Ammonia by Multiheme Cytochromes c

2014
The global biogeochemical nitrogen cycle is essential for life on Earth. Many of the underlying biotic reactions are catalyzed by a multitude of prokaryotic and eukaryotic life forms whereas others are exclusively carried out by microorganisms. The last century has seen the rise of a dramatic imbalance in the global nitrogen cycle due to human behavior
Jörg, Simon, Peter M H, Kroneck
openaire   +2 more sources

Production of Recombinant Multiheme Cytochromes c in Wolinella succinogenes

2011
Respiratory nitrogen cycle processes like nitrification, nitrate reduction, denitrification, nitrite ammonification, or anammox involve a variety of dissimilatory enzymes and redox-active cofactors. In this context, an intriguing protein class are cytochromes c, that is, enzymes containing one or more covalently bound heme groups that are attached to ...
Melanie, Kern, Jörg, Simon
openaire   +2 more sources

NMR and visible spectroscopy characterization of the redox behaviour of a multiheme cytochrome

Journal of Inorganic Biochemistry, 1989
J Legall
exaly   +2 more sources

Tools for resolving complexity in the electron transfer networks of multiheme cytochromes c

Metallomics, 2011
Examining electron transfer between two proteins with identical spectroscopic signatures is a challenging task. It is supposed that several multiheme cytochromes in Shewanella oneidensis form a molecular "wire" through which electrons are transported across the cellular space and a direct study of this transient protein-protein interaction has not yet ...
Mackenzie A, Firer-Sherwood, Kathryn D, Bewley, Jee-Young, Mock, Sean J, Elliott   +3 more
openaire   +2 more sources

Conformational properties of multihemic cytochromes c from Desulfuromonas acetoxidans

Thermochimica Acta, 2003
Abstract In the classification of c-type cytochromes, the class III includes multihemic cytochromes c with low redox potential constituting the cytochrome c3 superfamily. Most of the cytochromes described have been isolated from sulfate or sulfur reducing bacteria.
M.T. Giudici-Orticoni, A.A. Makarov, V.M. Lobachov, I.I. Protasevich, D. Lexa, M. Bruschi   +5 more
openaire   +1 more source