Results 121 to 130 of about 849 (155)
Some of the next articles are maybe not open access.
Springer Briefs in Molecular Science, 2016
Joana M. Dantas, Carlos A. Salgueiro
exaly +5 more sources
Joana M. Dantas, Carlos A. Salgueiro
exaly +5 more sources
A New Paradigm of Multiheme Cytochrome Evolution by Grafting and Pruning Protein Modules. [PDF]
Molecular Biology and Evolution, 2022 Abstract Multiheme cytochromes play key roles in diverse biogeochemical cycles, but understanding the origin and evolution of these proteins is a challenge due to their ancient origin and complex structure. Up until now, the evolution of multiheme cytochromes composed by multiple redox modules in a single polypeptide chain was ...
Ricardo Soares +2 more
exaly +3 more sources
Photosensitised Multiheme Cytochromes as Light-Driven Molecular Wires and Resistors [PDF]
ChemBioChem, 2018 AbstractMultiheme cytochromes possess closely packed redox‐active hemes arranged as chains spanning the tertiary structure. Here we describe five variants of a representative multiheme cytochrome engineered as biohybrid phototransducers for converting light into electricity.
Nicholas Watmough +2 more
exaly +5 more sources
Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR
Chemical Communications, 2014Residual 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 +3 more
openaire +2 more sources
A systematic investigation of multiheme c-type cytochromes in prokaryotes
JBIC Journal of Biological Inorganic Chemistry, 2010Multiheme 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 +2 more
openaire +3 more sources
Biochemistry, 2022
The multiheme cytochrome MtrA enables microbial respiration by transferring electrons across the outer membrane to extracellular electron acceptors. While structural studies have identified residues that mediate MtrA binding to hemes and to other cytochromes that facilitate extracellular electron transfer (EET), the relative ...
Ian J. Campbell +6 more
openaire +2 more sources
The multiheme cytochrome MtrA enables microbial respiration by transferring electrons across the outer membrane to extracellular electron acceptors. While structural studies have identified residues that mediate MtrA binding to hemes and to other cytochromes that facilitate extracellular electron transfer (EET), the relative ...
Ian J. Campbell +6 more
openaire +2 more sources
Resonance Raman fingerprinting of multiheme cytochromes from the cytochrome c 3 family
JBIC Journal of Biological Inorganic Chemistry, 2005Resonance 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 +5 more
openaire +2 more sources
The Production of Ammonia by Multiheme Cytochromes c
2014The 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
Structural and functional insights of GSU0105, a unique multiheme cytochrome from G. sulfurreducens
Biophysical Journal, 2021Geobacter 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. +4 more
openaire +2 more sources
Production of Recombinant Multiheme Cytochromes c in Wolinella succinogenes
2011Respiratory 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