Search Results - "Siebel, Judith F"

Direct Observation of an Iron-Bound Terminal Hydride in [FeFe]-Hydrogenase by Nuclear Resonance Vibrational Spectroscopy by Reijerse, Edward J, Pham, Cindy C, Pelmenschikov, Vladimir, Gilbert-Wilson, Ryan, Adamska-Venkatesh, Agnieszka, Siebel, Judith F, Gee, Leland B, Yoda, Yoshitaka, Tamasaku, Kenji, Lubitz, Wolfgang, Rauchfuss, Thomas B, Cramer, Stephen P

“…[FeFe]-hydrogenases catalyze the reversible reduction of protons to molecular hydrogen with extremely high efficiency. The active site (“H-cluster”) consists…”
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Spectroscopic Characterization of the Bridging Amine in the Active Site of [FeFe] Hydrogenase Using Isotopologues of the H‑Cluster by Adamska-Venkatesh, Agnieszka, Roy, Souvik, Siebel, Judith F, Simmons, Trevor R, Fontecave, Marc, Artero, Vincent, Reijerse, Edward, Lubitz, Wolfgang

“…The active site of [FeFe] hydrogenase contains a catalytic binuclear iron subsite coordinated by CN– and CO ligands as well as a unique azadithiolate (adt2–)…”
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Artificially maturated [FeFe] hydrogenase from Chlamydomonas reinhardtii: a HYSCORE and ENDOR study of a non-natural H-cluster by Adamska-Venkatesh, Agnieszka, Simmons, Trevor R, Siebel, Judith F, Artero, Vincent, Fontecave, Marc, Reijerse, Edward, Lubitz, Wolfgang

“…Hydrogenases are enzymes that catalyze the oxidation of H2 as well as the reduction of protons to form H2. The active site of [FeFe] hydrogenase is referred to…”
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Hybrid [FeFe]-Hydrogenases with Modified Active Sites Show Remarkable Residual Enzymatic Activity by Siebel, Judith F, Adamska-Venkatesh, Agnieszka, Weber, Katharina, Rumpel, Sigrun, Reijerse, Edward, Lubitz, Wolfgang

“…[FeFe]-hydrogenases are to date the only enzymes for which it has been demonstrated that the native inorganic binuclear cofactor of the active site…”
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Spectroscopic Investigations of [FeFe] Hydrogenase Maturated with [(57)Fe2(adt)(CN)2(CO)4](2-) by Gilbert-Wilson, Ryan, Siebel, Judith F, Adamska-Venkatesh, Agnieszka, Pham, Cindy C, Reijerse, Edward, Wang, Hongxin, Cramer, Stephen P, Lubitz, Wolfgang, Rauchfuss, Thomas B

“…The preparation and spectroscopic characterization of a CO-inhibited [FeFe] hydrogenase with a selectively (57)Fe-labeled binuclear subsite is described. The…”
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Structural Insight into the Complex of Ferredoxin and [FeFe] Hydrogenase from Chlamydomonas reinhardtii by Rumpel, Sigrun, Siebel, Judith F., Diallo, Mamou, Farès, Christophe, Reijerse, Edward J., Lubitz, Wolfgang

“…The transfer of photosynthetic electrons by the ferredoxin PetF to the [FeFe] hydrogenase HydA1 in the microalga Chlamydomonas reinhardtii is a key step in…”
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Spectroscopic Investigations of [FeFe] Hydrogenase Maturated with [57Fe2(adt)(CN)2(CO)4]2 by Gilbert-Wilson, Ryan, Siebel, Judith F, Adamska-Venkatesh, Agnieszka, Pham, Cindy C, Reijerse, Edward, Wang, Hongxin, Cramer, Stephen P, Lubitz, Wolfgang, Rauchfuss, Thomas B

“…The preparation and spectroscopic characterization of a CO-inhibited [FeFe] hydrogenase with a selectively 57Fe-labeled binuclear subsite is described. The…”
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Metal Selectivity of the Escherichia coli Nickel Metallochaperone, SlyD by Kaluarachchi, Harini, Siebel, Judith F, Kaluarachchi-Duffy, Supipi, Krecisz, Sandra, Sutherland, Duncan E. K, Stillman, Martin J, Zamble, Deborah B

“…SlyD is a Ni(II)-binding protein that contributes to nickel homeostasis in Escherichia coli. The C-terminal domain of SlyD contains a rich variety of…”
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Insertion of Heme b into the Structure of the Cys34‐Carbamidomethylated Human Lipocalin α 1 ‐Microglobulin: Formation of a [(Heme) 2 (α 1 ‐Microglobulin)] 3 Complex by Siebel, Judith F., Kosinsky, Robyn L., Åkerström, Bo, Knipp, Markus

“…α 1 ‐Microglobulin (α 1 m) is a 26 kDa plasma and tissue protein belonging to the lipocalin protein family. Previous investigations indicate that the protein…”
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Insertion of Heme b into the Structure of the Cys34-Carbamidomethylated Human Lipocalin a1-Microglobulin: Formation of a [(Heme)2(a1-Microglobulin)]3 Complex by Siebel, Judith F., Kosinsky, Robyn L., Åkerström, Bo, Knipp, Markus

“…a1-Microglobulin (a1m) is a 26 kDa plasma and tissue protein belonging to the lipocalin protein family. Previous investigations indicate that the protein…”
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Insertion of Heme b into the Structure of the Cys34-Carbamidomethylated Human Lipocalin α1-Microglobulin: Formation of a [(Heme)2(α1-Microglobulin)]3 Complex by Siebel, Judith F., Kosinsky, Robyn L., Åkerström, Bo, Knipp, Markus

“…α1‐Microglobulin (α1m) is a 26 kDa plasma and tissue protein belonging to the lipocalin protein family. Previous investigations indicate that the protein…”
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Metal selectivity of the E. coli nickel metallochaperone, SlyD by Kaluarachchi, Harini, Siebel, Judith F., Kaluarachchi-Duffy, Supipi, Krecisz, Sandra, Sutherland, Duncan E. K., Stillman, Martin J., Zamble, Deborah B.

“…SlyD is a Ni(II)-binding protein that contributes to nickel homeostasis in Escherichia coli . The C-terminal domain of SlyD contains a rich variety of…”
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Insertion of heme b into the structure of the Cys34-carbamidomethylated human lipocalin α(1)-microglobulin: formation of a [(heme)(2) (α(1)-Microglobulin)](3) complex by Siebel, Judith F, Kosinsky, Robyn L, Åkerström, Bo, Knipp, Markus

“…α(1)-Microglobulin (α(1)m) is a 26 kDa plasma and tissue protein belonging to the lipocalin protein family. Previous investigations indicate that the protein…”
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