Zobrazeno 1 - 10
of 70
pro vyhledávání: '"James B. Howard"'
Autor:
Rebeccah A. Warmack, Ailiena O. Maggiolo, Andres Orta, Belinda B. Wenke, James B. Howard, Douglas C. Rees
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-10 (2023)
Abstract Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia during the process of biological nitrogen fixation that is essential for sustaining life. The active site FeMo-cofactor contains a [7Fe:1Mo:9S:1C] metallocluster coor
Externí odkaz:
https://doaj.org/article/be832672eab34ef78cf20fb18ca4bfdc
Publikováno v:
eLife, Vol 4 (2015)
Dinitrogen reduction in the biological nitrogen cycle is catalyzed by nitrogenase, a two-component metalloenzyme. Understanding of the transformation of the inert resting state of the active site FeMo-cofactor into an activated state capable of reduc
Externí odkaz:
https://doaj.org/article/0cdb2a0894bb42d2ba78050463fd7b8d
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e72751 (2013)
Amino acid residues critical for a protein's structure-function are retained by natural selection and these residues are identified by the level of variance in co-aligned homologous protein sequences. The relevant residues in the nitrogen fixation Co
Externí odkaz:
https://doaj.org/article/3603777c621042f3a66a83315c82155f
Publikováno v:
Biochemistry
Proton uptake accompanies the reduction of all known substrates by nitrogenase. As a consequence, a higher pH should limit the availability of protons as a substrate essential for turnover, thereby increasing the proportion of more highly reduced for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::141a46b7f7f443c62c927ef968431fc7
https://doi.org/10.1021/bi4014769
https://doi.org/10.1021/bi4014769
Autor:
Kun Yun Yang, Limei Zhang, Jens T. Kaiser, Douglas C. Rees, James B. Howard, Thomas Spatzal, Oliver Einsle, Gabriele Meloni, Susana L. A. Andrade
Publikováno v:
Angewandte Chemie International Edition. 52:10529-10532
Another iron in the fire: X-ray anomalous diffraction studies on the nitrogenase MoFe protein show the presence of a mononuclear iron site, designated as Fe16, which was previously identified as either Ca^(2+) or Mg^(2+). The position of the absorpti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4051eaa645ebdb6a8c7c2ddcf57ebe08
https://doi.org/10.1002/anie.201303877
https://doi.org/10.1002/anie.201303877
Publikováno v:
eLife
eLife, Vol 4 (2015)
eLife, Vol 4 (2015)
Dinitrogen reduction in the biological nitrogen cycle is catalyzed by nitrogenase, a two-component metalloenzyme. Understanding of the transformation of the inert resting state of the active site FeMo-cofactor into an activated state capable of reduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5cf7e0640a7898ba105cd54ee7710c8
http://europepmc.org/articles/PMC4755756
http://europepmc.org/articles/PMC4755756
Autor:
Douglas C. Rees, Mika Y. Walton, Debarshi Mustafi, F. Akif Tezcan, Jens T. Kaiser, James B. Howard
Publikováno v:
Science. 309:1377-1380
Adenosine triphosphate (ATP) hydrolysis in the nitrogenase complex controls the cycle of association and dissociation between the electron donor adenosine triphosphatase (ATPase) (Fe-protein) and its target catalytic protein (MoFe-protein), driving t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b416062cb181079c6c9983dec972e13f
https://doi.org/10.1126/science.1115653
https://doi.org/10.1126/science.1115653
Autor:
James B. Howard, Susana L. A. Andrade, F. Akif Tezcan, Douglas C. Rees, Mika Y. Walton, Chad A. Haynes, Oliver Einsle
Publikováno v:
Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences. 363:971-984
Biological nitrogen fixation is mediated by the nitrogenase enzyme system that catalyses the ATP dependent reduction of atmospheric dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the MoFe-protein with the FeMo-cofactor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::477d069a747d1572dba2b61568c1cdd8
https://doi.org/10.1098/rsta.2004.1539
https://doi.org/10.1098/rsta.2004.1539
Autor:
Andreas Willing, James B. Howard, Benedikt Schmid, Oliver Einsle, Mika Yoshida, Hsiu-Ju Chiu, Douglas C. Rees
Publikováno v:
Biochemistry. 41:15557-15565
The transient formation of a complex between the component Fe- and MoFe-proteins of nitrogenase represents a central event in the substrate reduction mechanism of this enzyme. Previously, we have isolated an N-[3-(dimethylamino)propyl]-N'-ethylcarbod
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f126e5818d2e1501295c3862dec37524
https://doi.org/10.1021/bi026642b
https://doi.org/10.1021/bi026642b