Výsledky vyhledávání - "Jeremiah N, Betz"

HydG, the 'dangler' iron, and catalytic production of free CO and CN−: implications for [FeFe]-hydrogenase maturation

Autor: Elizabeth C. McDaniel, Jeremiah N. Betz, William E. Broderick, Joan B. Broderick, Adrien Pagnier, Eric M. Shepard, John W. Peters, Amanda S. Byer, Stella Impano, Amanda Galambas, Hope Watts, Kaitlin S. Duschene, Benjamin R. Duffus, Shawn E. McGlynn

Publikováno v: Dalton Transactions. 50:10405-10422

The organometallic H-cluster of the [FeFe]-hydrogenase consists of a [4Fe-4S] cubane bridged via a cysteinyl thiolate to a 2Fe subcluster ([2Fe]H) containing CO, CN-, and dithiomethylamine (DTMA) ligands. The H-cluster is synthesized by three dedicat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b3bcff9b8c51cdf25076b11b64769e81
https://doi.org/10.1039/d1dt01359a

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HydG, the 'dangler' iron, and catalytic production of free CO and CN

Autor: Eric M, Shepard, Stella, Impano, Benjamin R, Duffus, Adrien, Pagnier, Kaitlin S, Duschene, Jeremiah N, Betz, Amanda S, Byer, Amanda, Galambas, Elizabeth C, McDaniel, Hope, Watts, Shawn E, McGlynn, John W, Peters, William E, Broderick, Joan B, Broderick

Publikováno v: Dalton Trans

The organometallic H-cluster of the [FeFe]-hydrogenase consists of a [4Fe–4S] cubane bridged via a cysteinyl thiolate to a 2Fe subcluster ([2Fe](H)) containing CO, CN(−), and dithiomethylamine (DTMA) ligands. The H-cluster is synthesized by three

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b1bae996cd2b917f0d074847f2875cd2
https://pubmed.ncbi.nlm.nih.gov/34240096

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Electron Spin Relaxation and Biochemical Characterization of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S] Cluster Communication and Hydrogenase Activation

Autor: Robert J. Usselman, Joan B. Broderick, Krista A. Shisler, Eric M. Shepard, Jeremiah N. Betz, Priyanka Aggarwal, Gareth R. Eaton, Amanda S. Byer, Anna G. Scott, Sandra S. Eaton

Publikováno v: Biochemistry

Nature utilizes [FeFe]-hydrogenase enzymes to catalyze the interconversion between H2 and protons and electrons. Catalysis occurs at the H-cluster, a carbon monoxide-, cyanide-, and dithiomethylamine-coordinated 2Fe subcluster bridged via a cysteine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebec9820ca6ef2b9b3a2f1a97b65f9b8
https://doi.org/10.1021/acs.biochem.7b00169

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H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG

Autor: Eric M. Shepard, Amanda S. Byer, Paul W. King, William E. Broderick, Joan B. Broderick, Jeremiah N. Betz, Michael W. Ratzloff

Publikováno v: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 24(6)

[FeFe]-hydrogenase catalyzes the reversible reduction of protons to H2 at a complex metallocofactor site, the H-cluster. Biosynthesis of this active-site H-cluster requires three maturation enzymes: the radical S-adenosylmethionine enzymes HydE and H

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1f370f38e8f4b3e5617d3076b6adbd0
https://pubmed.ncbi.nlm.nih.gov/31493152

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A Redox Active [2Fe-2S] Cluster on the Hydrogenase Maturase HydF

Autor: Jeremiah N. Betz, Eric M. Shepard, Joan B. Broderick, John W. Peters, Amanda S. Byer

Publikováno v: Biochemistry. 55:3514-3527

[FeFe]-hydrogenases are nature’s most prolific hydrogen catalysts, excelling at facilely interconverting H2 and protons. The catalytic core common to all [FeFe]-hydrogenases is a complex metallocofactor, referred to as the H-cluster, which is compo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9367016d50a8b15a0a657a749755f05e
https://doi.org/10.1021/acs.biochem.6b00528

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[FeFe]-Hydrogenase Maturation

Autor: Jeremiah N. Betz, Florence Mus, Joan B. Broderick, Amanda S. Byer, Eric M. Shepard, John W. Peters, Benjamin R. Duffus

Publikováno v: Biochemistry. 53:4090-4104

Hydrogenases are metalloenzymes that catalyze the reversible reduction of protons at unusual metal centers. This Current Topic discusses recent advances in elucidating the steps involved in the biosynthesis of the complex metal cluster at the [FeFe]-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30869e1f38b94fff603cb2df39978c59
https://doi.org/10.1021/bi500210x

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Further Insight into the Nature of Ball-Lightning-Like Atmospheric Pressure Plasmoids

Autor: Jeremiah N. Betz, C. Michael Lindsay, David M. Friday, Peter B. Broughton, Tanner A. Lee, Garrett A. Schutz

Publikováno v: The Journal of Physical Chemistry A. 117:9931-9940

Known since antiquity, ball lightning is a natural, long-lived plasma-like phenomenon associated with thunderstorms and is not well understood due to its rarity and unpredictability. A recently discovered laboratory phenomenon with striking similarit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f88755650979d8c9228a3fbbdbbaa2fb
https://doi.org/10.1021/jp400001y

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[FeFe]-hydrogenase maturation: insights into the role HydE plays in dithiomethylamine biosynthesis

Autor: Eyal Akiva, Corey J. Fugate, Joan B. Broderick, Patricia C. Babbitt, Eric M. Shepard, Gemma L. Holliday, Anna G. Scott, Jeremiah N. Betz, John W. Peters, Nicholas W. Boswell

Publikováno v: Biochemistry, vol 54, iss 9

HydE and HydG are radical S-adenosyl-l-methionine enzymes required for the maturation of [FeFe]-hydrogenase (HydA) and produce the nonprotein organic ligands characteristic of its unique catalytic cluster. The catalytic cluster of HydA (the H-cluster

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70bcde8f7b8a7ec14c38bb08ea4fbc43
https://pubmed.ncbi.nlm.nih.gov/25654171

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H-cluster assembly during maturation of the [FeFe]-hydrogenase

Autor: Eric M. Shepard, Jeremiah N. Betz, Amanda S. Byer, Kaitlin S. Duschene, John W. Peters, Benjamin R. Duffus, Joan B. Broderick

Publikováno v: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 19(6)

The organometallic H-cluster at the active site of the [FeFe]-hydrogenase serves as the site of reversible binding and reduction of protons to produce H2. The H-cluster is unique in biology, and consists of a 2Fe subcluster tethered to a typical [4Fe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0711b555eec8f45d9c986ca00eea68d7
https://pubmed.ncbi.nlm.nih.gov/24972661

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