Zobrazeno 1 - 10
of 88
pro vyhledávání: '"Mark S. Hargrove"'
Autor:
Nathan L. Bandow, Jeremy D. Semrau, Matheus Fonseca, Junwon Yang, Mark S. Hargrove, Alan A. DiSpirito, Hans Zischka, Thomas A. Bobik, Marcus T. McEllistrem, Ana M DiSpirito, Rafael A Heinze, Jacob R Jennett, Navjot Singh Athwal, Philip Dershwitz, Joshua C Ledesma
Publikováno v:
Appl. Environ. Microbiol. 87:e00286-21 (2021)
Applied and Environmental Microbiology
Applied and Environmental Microbiology
Methanobactins (MBs) are small (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b83081081912beeb9c8ecac014894c4
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=61926
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=61926
Autor:
Xiaoguang Wang, Mark S Hargrove
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e82611 (2013)
Ascorbic acid and hemoglobins have been linked to nitric oxide metabolism in plants. It has been hypothesized that ascorbic acid directly reduces plant hemoglobin in support of NO scavenging, producing nitrate and monodehydroascorbate. In this scenar
Externí odkaz:
https://doaj.org/article/4a3bb73bcfaa4a809ab31e5c1a29d19e
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
18 Pags.- 1 Tabl.- 7 Figs. © 2020 The Authors. Under Creative Commons License Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0).
Globins (Glbs) are widely distributed in archaea, bacteria and eukaryotes. They can be cl
Globins (Glbs) are widely distributed in archaea, bacteria and eukaryotes. They can be cl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29e91e2a7469320e65e7ff8b1cd796ae
http://hdl.handle.net/10261/219101
http://hdl.handle.net/10261/219101
Autor:
Nicole Frankenberg-Dinkel, Mark S. Hargrove, Masanori Sono, Anuja Modi, Shengfang Sun, John H. Dawson, Bastian Molitor
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 23:1085-1092
The binding of neutral thiol (ethanethiol, EtSH) or thioether (tetrahydrothiophene, THT) to two types of heme proteins in their ferrous state has been investigated with UV-visible (UV-Vis) absorption and magnetic circular dichroism spectroscopy. For
Publikováno v:
PLoS ONE, Vol 3, Iss 4, p e2039 (2008)
Genomics has produced hundreds of new hemoglobin sequences with examples in nearly every living organism. Structural and biochemical characterizations of many recombinant proteins reveal reactions, like oxygen binding and NO dioxygenation, that appea
Externí odkaz:
https://doaj.org/article/317fc8694e2d4ec68f1015c1807156ca
Publikováno v:
Biochemistry. 55:5809-5817
Reduction of hydroxylamine to ammonium by phytoglobin, a plant hexacoordinate hemoglobin, is much faster than that of other hexacoordinate hemoglobins or pentacoordinate hemoglobins such as myoglobin, leghemoglobin, and red blood cell hemoglobin. The
Autor:
Denis Tamiev, Jagannathan Alagurajan, Alan A. DiSpirito, Xiaoguang Wang, Gregory J. Phillips, Mark S. Hargrove
Publikováno v:
Archives of microbiology. 201(4)
Nitrate and nitrite reduction are of paramount importance for nitrogen assimilation and anaerobic metabolism, and understanding the specific roles of each participating reductase is necessary to describe the biochemical balance that dictates cellular
Autor:
Jagannathan Alagurajan, Mark S. Hargrove, Navjot Singh Athwal, Amy H. Andreotti, Ryan Sturms, D. Bruce Fulton
Publikováno v:
Journal of Inorganic Biochemistry. 150:139-147
Hemoglobins (phytoglobins) from rice plants (nsHb1) and from the cyanobacterium Synechocystis (PCC 6803) (SynHb) can reduce hydroxylamine with two electrons to form ammonium. The reaction requires intermolecular electron transfer between protein mole
Publikováno v:
F1000Research
Hemoglobin (Hb) is a heme-containing protein found in the red blood cells of vertebrates. For many years, the only known Hb-like molecule in plants was leghemoglobin (Lb). The discovery that other Hb-like proteins existed in plants led to the term
Publikováno v:
Biochemistry. 50:3873-3878
The ability of ferrous hemoglobins to reduce nitrite to form nitric oxide has been demonstrated for hemoglobins from animals, including myoglobin, blood cell hemoglobin, neuroglobin, and cytoglobin. In all cases, the rate constants for the bimolecula