Conjuring up a ghost: structural and functional characterization of FhuF, a ferric siderophore reductase from E. coli

Autor: Estelle Lebègue, T Cordeiro, Frédéric Barrière, Inês B. Trindade, G Hernandez, Mario Piccioli, Ricardo O. Louro

Publikováno v: Journal of Biological Inorganic Chemistry
Journal of Biological Inorganic Chemistry, 2021, 26 (2-3), pp.313-326. ⟨10.1007/s00775-021-01854-y⟩
Journal of Biological Inorganic Chemistry, Springer Verlag, 2021, ⟨10.1007/s00775-021-01854-y⟩
J Biol Inorg Chem

Graphic abstract Iron is a fundamental element for virtually all forms of life. Despite its abundance, its bioavailability is limited, and thus, microbes developed siderophores, small molecules, which are synthesized inside the cell and then released

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1e06fe4321cbd6185fba9f52d868b4e
http://europepmc.org/articles/PMC8068687

Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From

Autor: Liliana R, Teixeira, Cristina M, Cordas, Marta P, Fonseca, Norma E C, Duke, Phani Raj, Pokkuluri, Carlos A, Salgueiro

Publikováno v: Frontiers in Microbiology

The monoheme outer membrane cytochrome F (OmcF) from Geobacter sulfurreducens plays an important role in Fe(III) reduction and electric current production. The electrochemical characterization of this cytochrome has shown that its redox potential is

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::913c0ae3eb3d9579dc62b29c65f8118d
https://pubmed.ncbi.nlm.nih.gov/32010071

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Redox Bohr effects and the role of heme a in the proton pump of bovine heart cytochrome c oxidase

Autor: Nazzareno Capitanio, Pietro Luca Martino, Sergio Papa, Giuseppe Capitanio

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1807:1287-1294

Structural and functional observations are reviewed which provide evidence for a central role of redox Bohr effect linked to the low-spin heme a in the proton pump of bovine heart cytochrome c oxidase. Data on the membrane sidedness of Bohr protons l

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fad763a554795105c61dd4a9f5e1e5b7
https://doi.org/10.1016/j.bbabio.2011.02.004

Cytochrome c″ from the obligate methylotroph Methylophilus methylotrophus, an unexpected homolog of sphaeroides heme protein from the phototroph Rhodobacter sphaeroides

Autor: Klaus Klarskov, David Leys, Helena S. Costa, Jozef Van Beeumen, K. Backers, Helena Santos, Yves Guisez

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1412(1):47-55

The complete primary structure of an unusual soluble cytochrome c isolated from the obligate methylotrophic bacterium Methylophilus methylotrophus has been determined to contain 124 amino acids and to have an average molecular mass of 14 293.0 Da. Th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d33061cfbc3787337a52b4e06e612aa