Results 51 to 60 of about 414,309 (352)

Staphylococcus aureus HemX Modulates Glutamyl-tRNA Reductase Abundance To Regulate Heme Biosynthesis

mBio, 2018
Staphylococcus aureus is responsible for a significant amount of devastating disease. Its ability to colonize the host and cause infection is supported by a variety of proteins that are dependent on the cofactor heme.
Jacob E. Choby, Caroline M. Grunenwald, Arianna I. Celis, Svetlana Y. Gerdes, Jennifer L. DuBois, Eric P. Skaar   +5 more
doaj   +1 more source

Resolution of Key Roles for the Distal Pocket Histidine in Cytochrome c Nitrite Reductases [PDF]

, 2015
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, Butt, Julea, Cheesman, Myles, Clarke, Tom, Kern, Melanie, Lockwood, Colin, Richardson, David, Simon, Jorg   +7 more
core   +5 more sources

Structure and function of the bacterial heterodimeric ABC transporter CydDC: stimulation of ATPase activity by thiol and heme compounds. [PDF]

, 2014
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, Booth, WI, Bullough, PA, Nyathi, Y, Poole, RK, Postis, V, Shepherd, M, Tzokov, SB, Xie, H, Yamashita, M   +9 more
core   +3 more sources

A Diffusion-Based Approach to Geminate Recombination of Heme Proteins with Small Ligands [PDF]

, 2002
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, Anfinrud, Ansari, Ansari, Antonioni, Austin, Baldwin, Berlin, Bonaventura, Bruha, Cameron, Case, Chernoff, Cotes, Dadusc, Das, Dasgupta, Doster, Dzhagarov, Dzhagarov, Dzhagarov, Dzhagarov, Eaton, Elber, Fermi, Frauenfelder, Frauenfelder, Frauenfelder, Gallo, Gibson, Gibson, Hasinoff, Henry, Ho, Horbach, Johnson, Johnson, Jost, Kimanaka, Kottalam, Kuczera, Lepeshkevich, Lim, Lindqvist, Lukin, Marden, Morris, Muller, Murray, Olson, Olson, Perutz, Perutz, Perutz, Petrich, Potter, Quillin, Rifkind, Rodgers, Schaad, Schlichting, Shaanan, Springer, Starovoitov, Steinbach, Steinbach, Straub, Yamamoto, Yang, Ye   +69 more
core   +2 more sources

Control of intracellular heme levels: Heme transporters and heme oxygenases

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2011
Heme serves as a co-factor in proteins involved in fundamental biological processes including oxidative metabolism, oxygen storage and transport, signal transduction and drug metabolism. In addition, heme is important for systemic iron homeostasis in mammals.
Khan, Anwar A., Quigley, John G.
openaire   +2 more sources

The heme-responsive PrrH sRNA regulates Pseudomonas aeruginosa pyochelin gene expression

mSphere, 2023
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, Weiliang Huang, Jonathan Gans, Jacob Weiner, Evan Nowak, Mariette Barbier, Angela Wilks, Maureen A. Kane, Amanda G. Oglesby   +8 more
doaj   +1 more source

Heme Oxygenase-1 Expression Affects Murine Abdominal Aortic Aneurysm Progression. [PDF]

, 2016
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, Dalman, Ronald L, Deng, Alicia C, Hsu, Mark, Kalish, Flora, Kayama, Yosuke, Maegdefessel, Lars, Morisawa, Takeshi, Spin, Joshua M, Stevenson, David K, Tsao, Philip S, Wallenstein, Matthew B, Wong, Ronald J, Zhao, Hui   +13 more
core   +2 more sources

Free Rather Than Total Iron Content Is Critically Linked to the Fur Physiology in Shewanella oneidensis

Frontiers in Microbiology, 2020
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, Xue Feng, Wei Wang, Yining Chen, Zhe Chen, Haichun Gao   +5 more
doaj   +1 more source

Import of cytochrome c into mitochondria [PDF]

, 1987
The import of cytochrome c into mitochondria can be resolved into a number of discrete steps. Here we report on the covalent attachment of heme to apocytochrome c by the enzyme cytochrome c heme lyase in mitochondria from Neurospora crassa. A new method
Basile G., Burnette W. N., Chance B., Dumont M. E., Ernst V., Estabrook R. W., Freitag H., Gasser S. M., Hackenbrock C. R., Hay R., Heller J., Hennig B., Hennig B., Hennig B., Kanarek L., Korb H., Laemmli U. K., Lederer F., Matner R. R., Matsuura S., Means G. E., Mihara K., Nicholson D. W., Nozaki M., Pelham H. R. B., Rietveld A., Rietveld A., Rietveld A., Rietveld A., Scarpulla R. C., Schmidt B., Sherman F., Stewart J. W., Taniuchi H., Taniuchi H., Towbin H., Veloso D., Visco C., Yuan P.-M., Zimmermann R., Zimmermann R., Zimmermann R., Zitomer R. S.   +42 more
core   +1 more source

A mutant of Neurospora crassa deficient in cytochrome c heme lyase activity cannot import cytochrome c into mitochondria [PDF]

, 1988
The nuclear cyt-2-1 mutant of Neurospora crassa is characterized by a gross deficiency of cytochrome c (Bertrand, H., and Collins, R. A. (1978) Mol. Gen. Genet. 166, 1-13).
Drygas, Mariola E., Kwong, Patrick L., Nargang, Frank E., Neupert, Walter, Nicholson, Donald W.   +4 more
core   +1 more source