Zobrazeno 1 - 10
of 234
pro vyhledávání: '"John D Lipscomb"'
Catalase (KatA) plays a role in protection against anaerobic nitric oxide in Pseudomonas aeruginosa.
Autor:
Shengchang Su, Warunya Panmanee, Jeffrey J Wilson, Harry K Mahtani, Qian Li, Bradley D Vanderwielen, Thomas M Makris, Melanie Rogers, Cameron McDaniel, John D Lipscomb, Randall T Irvin, Michael J Schurr, Jack R Lancaster, Rhett A Kovall, Daniel J Hassett
Publikováno v:
PLoS ONE, Vol 9, Iss 3, p e91813 (2014)
Pseudomonas aeruginosa (PA) is a common bacterial pathogen, responsible for a high incidence of nosocomial and respiratory infections. KatA is the major catalase of PA that detoxifies hydrogen peroxide (H2O2), a reactive oxygen intermediate generated
Externí odkaz:
https://doaj.org/article/2a9a2058cec142418a13cea117b0b81a
Publikováno v:
Biochemistry.
The hydroxylase component (S5HH) of salicylate-5-hydroxylase catalyzes C5 ring hydroxylation of salicylate but switches to methyl hydroxylation when a C5 methyl substituent is present. The use of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff42269d2e80e8283271f5954b07cfd5
https://pubmed.ncbi.nlm.nih.gov/36583545
https://pubmed.ncbi.nlm.nih.gov/36583545
Autor:
Kiyoung Park, Makoto Seto, Makina Saito, Ariel B. Jacobs, Jeffrey T. Babicz, Kenji Tamasaku, Leland B. Gee, Yoshitaka Yoda, Shinji Kitao, Kyle D. Sutherlin, Rahul Banerjee, John D. Lipscomb, Edward I. Solomon, Yasuhiro Kobayashi, Dory Ellen Deweese, Lars H. Böttger, Augustin Braun
Publikováno v:
Journal of the American Chemical Society. 143:16007-16029
Methanotrophic bacteria utilize the nonheme diiron enzyme soluble methane monooxygenase (sMMO) to convert methane to methanol in the first step of their metabolic cycle under copper-limiting conditions. The structure of the sMMO Fe(IV)2 intermediate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f3ff2368e60708a7a1db8c004634c10
https://doi.org/10.1021/jacs.1c05436
https://doi.org/10.1021/jacs.1c05436
Autor:
Alexander Strom, Rachit Shah, Rafal Dolot, Melanie S. Rogers, Cher-Ling Tong, David Wang, Youlin Xia, John D. Lipscomb, Carston R. Wagner
Publikováno v:
Biochemistry
Human histidine triad nucleotide binding (hHINT) proteins catalyze nucleotide phosphoramidase and acyl-phosphatase reactions that are essential for the activation of antiviral proTides, such as Sofosbuvir and Remdesivir. hHINT1 and hHINT2 are highly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64b9e98dddd1dac4219a4a1b7bb83d7e
https://europepmc.org/articles/PMC9854251/
https://europepmc.org/articles/PMC9854251/
Autor:
Rahul Banerjee, Manny M. Semonis, John D. Lipscomb, William C. K. Pomerantz, Jason C. Jones, Ke Shi, Hideki Aihara
Publikováno v:
Biochemistry
Soluble methane monooxygenase (sMMO) is a multicomponent metalloenzyme capable of catalyzing the fissure of the C-H bond of methane and the insertion of one atom of oxygen from O2 to yield methanol. Efficient multiple-turnover catalysis occurs only i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f6c94f5c59c6c75af80957585d369a8
https://doi.org/10.1021/acs.biochem.1c00293
https://doi.org/10.1021/acs.biochem.1c00293
Autor:
George E. Cutsail, Rahul Banerjee, Derek B. Rice, Olivia McCubbin Stepanic, John D. Lipscomb, Serena DeBeer
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 27(6)
Soluble methane monooxygenase (sMMO) facilitates the conversion of methane to methanol at a non-heme FeIV2 intermediate MMOHQ, which is formed in the active site of the sMMO hydroxylase component (MMOH) during the catalytic cycle. Other biological sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e6eca4eab9fc4f5e6199c82d4b19d3f
https://pubmed.ncbi.nlm.nih.gov/35988092
https://pubmed.ncbi.nlm.nih.gov/35988092
Publikováno v:
Biochemistry. 59:2946-2961
The metalloenzyme soluble methane monooxygenase (sMMO) consists of hydroxylase (sMMOH), regulatory (MMOB), and reductase components. When sMMOH forms a complex with MMOB, the rate constants are greatly increased for the sequential access of O2, proto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aeed21ffd022155544fae949b1eff683
https://doi.org/10.1021/acs.biochem.0c00459
https://doi.org/10.1021/acs.biochem.0c00459
Autor:
Ariel Benjamin, Jacobs, Rahul, Banerjee, Dory Ellen, Deweese, Augustin, Braun, Jeffrey Thomas, Babicz, Leland Bruce, Gee, Kyle David, Sutherlin, Lars Hendrik, Böttger, Yoshitaka, Yoda, Makina, Saito, Shinji, Kitao, Yasuhiro, Kobayashi, Makoto, Seto, Kenji, Tamasaku, John D, Lipscomb, Kiyoung, Park, Edward I, Solomon
Publikováno v:
J Am Chem Soc
Methanotrophic bacteria utilize the non-heme diiron enzyme soluble methane monooxygenase (sMMO) to convert methane to methanol in the first step of their metabolic cycle under copper-limiting conditions. The structure of the sMMO Fe(IV)(2) intermedia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::59200297f7502f24af709a413c16b064
https://pubmed.ncbi.nlm.nih.gov/34570980
https://pubmed.ncbi.nlm.nih.gov/34570980
Publikováno v:
Annual Review of Biochemistry. 88:409-431
Aerobic life is possible because the molecular structure of oxygen (O2) makes direct reaction with most organic materials at ambient temperatures an exceptionally slow process. Of course, these reactions are inherently very favorable, and they occur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e678fb929f8a21a97ab53c38afe1e682
https://doi.org/10.1146/annurev-biochem-013118-111529
https://doi.org/10.1146/annurev-biochem-013118-111529
Autor:
Rahul Banerjee, John D. Lipscomb
Publikováno v:
Acc Chem Res
Rigorous substrate selectivity is a hallmark of enzyme catalysis. This selectivity is generally ascribed to a thermodynamically favorable process of substrate binding to the enzyme active site based upon complementary physiochemical characteristics,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::590622031d38234f5a851ff014fbd8ad
https://pubmed.ncbi.nlm.nih.gov/33886257
https://pubmed.ncbi.nlm.nih.gov/33886257