A Heme Propionate Staples the Structure of Cytochrome c for Methionine Ligation to the Heme Iron

Autor: Madeline L Weaver, Kevin R. Hoke, Ekaterina V. Pletneva, Yunling Deng

Publikováno v: Inorganic Chemistry. 58:14085-14106

Ligand-switch reactions at the heme iron are common in biological systems, but their mechanisms and the features of the polypeptide fold that support dual ligation are not well understood. In cytochrome c (cyt c), two low-stability loops (Ω-loop C a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::44af80f9130e47e6f282ca3273bf1522
https://doi.org/10.1021/acs.inorgchem.9b02111

A Heme Propionate Staples the Structure of Cytochrome

Autor: Yunling, Deng, Madeline L, Weaver, Kevin R, Hoke, Ekaterina V, Pletneva

Publikováno v: Inorg Chem

Ligand-switch reactions at the heme iron are common in biological systems, but their mechanisms and the features of the polypeptide fold that support dual ligation are not well understood. In cytochrome c (cyt c), two low-stability loops (Ω-loop C a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b4cdb5a33eef58ccde770e844c5142ba
https://pubmed.ncbi.nlm.nih.gov/31589413

A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch

Autor: Ekaterina V. Pletneva, Kevin R. Hoke, Michael Q. Zhu, Stephanie L. Alden, George P. Lisi, Dean R. Madden, Jeanine F. Amacher, Fangfang Zhong

Publikováno v: Journal of the American Chemical Society. 137:8435-8449

It has been suggested that the alkaline form of cytochrome c (cyt c) regulates function of this protein as an electron carrier in oxidative phosphorylation and as a peroxidase that reacts with cardiolipin (CL) during apoptosis. In this form, Met80, t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8c3e58d92d1f122542cf0303f221cfe
https://doi.org/10.1021/jacs.5b01493

SOAS: A free program to analyze electrochemical data and other one-dimensional signals

Autor: Hendrik A. Heering, Kevin R. Hoke, Fanny Leroux, Carole Baffert, Patrick Bertrand, Vincent Fourmond, Christophe Léger

Publikováno v: Bioelectrochemistry and Bioenergetics
Bioelectrochemistry and Bioenergetics, Elsevier, 2009, ahead of print, ahead of print. ⟨10.1016/j.bioelechem.2009.02.010⟩
Bioelectrochemistry and Bioenergetics, 2009, ahead of print, ahead of print. ⟨10.1016/j.bioelechem.2009.02.010⟩

International audience; This paper describes an open source program called SOAS, which we developed with the aim of analysing one-dimensional signals. It offers a large set of commands for handling voltammetric and chronoamperometric data, including

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51cf14ed94253b1d3aac90a065aa2368
https://doi.org/10.1016/j.bioelechem.2009.02.010

Voltammetric Studies of the Catalytic Mechanism of the Respiratory Nitrate Reductase from Escherichia coli: How Nitrate Reduction and Inhibition Depend on the Oxidation State of the Active Site

Autor: Kerensa Heffron, Richard A. Rothery, Monica Palak, Fraser A. Armstrong, Joel H. Weiner, Sean Elliott, Kevin R. Hoke

Publikováno v: Biochemistry. 43:799-807

The respiratory molybdoenzyme nitrate reductase (NarGHI) from Escherichia coli has been studied by protein film voltammetry, with the enzyme adsorbed on a rotating disk pyrolytic graphite edge (PGE) electrode. Catalytic voltammograms for nitrate redu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc790403ff9c2114d151471fc181023b
https://doi.org/10.1021/bi035869j