Resolution of Key Roles for the Distal Pocket Histidine in Cytochrome c Nitrite Reductases [PDF]
Cytochrome c nitrite reductases perform a key step in the biogeochemical N-cycle by catalyzing the six-electron reduction of nitrite to ammonium. These multi-heme cytochromes contain a number of His/His ligated c-hemes for electron transfer and a ...
Burlat, Benedicte+7 more
core +4 more sources
A Dual Role of Heme Oxygenase-1 in Cancer Cells
Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions.
Shih-Kai Chiang+2 more
semanticscholar +1 more source
The heme-responsive PrrH sRNA regulates Pseudomonas aeruginosa pyochelin gene expression
Pseudomonas aeruginosa is an opportunistic pathogen that requires iron for growth and virulence, yet this nutrient is sequestered by the innate immune system during infection. When iron is limiting, P. aeruginosa expresses the PrrF1 and PrrF2 small RNAs (
Tra-My Hoang+8 more
doaj +1 more source
Structure and function of the bacterial heterodimeric ABC transporter CydDC: stimulation of ATPase activity by thiol and heme compounds. [PDF]
In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ATP-binding cassette-type cysteine/GSH transporter, CydDC.
Baldwin, SA+9 more
core +3 more sources
Ferric uptake regulator (Fur) is a transcriptional regulator playing a central role in iron homeostasis of many bacteria, and Fur inactivation commonly results in pleiotropic phenotypes.
Lulu Liu+5 more
doaj +1 more source
A Diffusion-Based Approach to Geminate Recombination of Heme Proteins with Small Ligands [PDF]
A model of postphotodissociative monomolecular (geminate) recombination of heme proteins with small ligands (NO, O2 or CO) is represented. The non-exponential decay with time for the probability to find a heme in unbound state is interpreted in terms of ...
Abadan+69 more
core +2 more sources
Nitric oxide binds to the proximal heme coordination site of the ferrocytochrome c/cardiolipin complex: formation mechanism and dynamics. [PDF]
Mammalian mitochondrial cytochrome c interacts with cardiolipin to form a complex (cyt. c/CL) important in apoptosis. Here we show that this interaction leads to structural changes in ferrocytochrome c that leads to an open coordinate site on the central
Husu, I+4 more
core +4 more sources
Heme Oxygenase-1 Expression Affects Murine Abdominal Aortic Aneurysm Progression. [PDF]
Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is a cytoprotective enzyme upregulated in the vasculature by increased flow and inflammatory stimuli.
Azuma, Junya+13 more
core +2 more sources
Maturation of Plastid c-type Cytochromes
Cytochromes c are hemoproteins, with the prosthetic group covalently linked to the apoprotein, which function as electron carriers. A class of cytochromes c is defined by a CXXCH heme-binding motif where the cysteines form thioether bonds with the vinyl ...
Stéphane T. Gabilly+3 more
doaj +1 more source
Endothelial TLR4 Expression Mediates Vaso-Occlusive Crisis in Sickle Cell Disease
Heme, released from red blood cells in sickle cell disease (SCD), interacts with toll-like receptor 4 (TLR4) to activate NF-κB leading to the production of cytokines and adhesion molecules which promote inflammation, pain, and vaso-occlusion.
Joan D. Beckman+11 more
doaj +1 more source