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Victor L Davidson

Showing results (91-100 of 109) with videos related to

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Biochemistry|February 14, 2007
Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic propertiesChristopher J Carrell, John K Ma, William E Antholine, et al.
Archives of Biochemistry and Biophysics|April 8, 2014
The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper siteBrian A Dow, Narayanasami Sukumar, Jason O Matos, et al.
Biochemistry|September 17, 2003
Chemical and kinetic reaction mechanisms of quinohemoprotein amine dehydrogenase from Paracoccus denitrificansDapeng Sun, Kazutoshi Ono, Toshihide Okajima, et al.
Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|September 25, 2003
X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551iZong-Xiang Xia, Wei-Wen Dai, Yong-Ning He, et al.
The Journal of Biological Chemistry|February 12, 2022
The hemerythrin-like diiron protein from Mycobacterium kansasii is a nitric oxide peroxidaseZhongxin Ma, Ashley A Holland, Ilana Szlamkowicz, et al.
Biochemistry|February 4, 2012
Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauGManliang Feng, Lyndal M R Jensen, Erik T Yukl, et al.
The Journal of Biological Chemistry|December 16, 2017
The Rv2633c protein of <i>Mycobacterium tuberculosis</i> is a non-heme di-iron catalase with a possible role in defenses against oxidative stressZhongxin Ma, Kyle T Strickland, Michelle D Cherne, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 5, 2011
Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesisNafez Abu Tarboush, Lyndal M R Jensen, Erik T Yukl, et al.
Molecules (Basel, Switzerland)|July 28, 2022
Structural Determinants of the Specific Activities of an L-Amino Acid Oxidase from <i>Pseudoalteromonas luteoviolacea</i> CPMOR-1 with Broad Substrate SpecificityKyle J Mamounis, Maria Luiza Caldas Nogueira, Daniela Priscila Marchi Salvador, et al.
Biochemistry|December 7, 2010
The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesisSooim Shin, Manliang Feng, Yan Chen, et al.
Pageof 11

Showing results (91-100 of 109) with videos related to

Sort By:
Pageof 11
Biochemistry|February 14, 2007
Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic propertiesChristopher J Carrell, John K Ma, William E Antholine, et al.
Archives of Biochemistry and Biophysics|April 8, 2014
The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper siteBrian A Dow, Narayanasami Sukumar, Jason O Matos, et al.
Biochemistry|September 17, 2003
Chemical and kinetic reaction mechanisms of quinohemoprotein amine dehydrogenase from Paracoccus denitrificansDapeng Sun, Kazutoshi Ono, Toshihide Okajima, et al.
Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|September 25, 2003
X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551iZong-Xiang Xia, Wei-Wen Dai, Yong-Ning He, et al.
The Journal of Biological Chemistry|February 12, 2022
The hemerythrin-like diiron protein from Mycobacterium kansasii is a nitric oxide peroxidaseZhongxin Ma, Ashley A Holland, Ilana Szlamkowicz, et al.
Biochemistry|February 4, 2012
Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauGManliang Feng, Lyndal M R Jensen, Erik T Yukl, et al.
The Journal of Biological Chemistry|December 16, 2017
The Rv2633c protein of <i>Mycobacterium tuberculosis</i> is a non-heme di-iron catalase with a possible role in defenses against oxidative stressZhongxin Ma, Kyle T Strickland, Michelle D Cherne, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 5, 2011
Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesisNafez Abu Tarboush, Lyndal M R Jensen, Erik T Yukl, et al.
Molecules (Basel, Switzerland)|July 28, 2022
Structural Determinants of the Specific Activities of an L-Amino Acid Oxidase from <i>Pseudoalteromonas luteoviolacea</i> CPMOR-1 with Broad Substrate SpecificityKyle J Mamounis, Maria Luiza Caldas Nogueira, Daniela Priscila Marchi Salvador, et al.
Biochemistry|December 7, 2010
The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesisSooim Shin, Manliang Feng, Yan Chen, et al.
Pageof 11