Výsledky vyhledávání - "Tadeo Moreno-Chicano"

Akademický článek

Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature

Publikováno v: IUCrJ, Vol 9, Iss 5, Pp 610-624 (2022)

Room-temperature macromolecular crystallography allows protein structures to be determined under close-to-physiological conditions, permits dynamic freedom in protein motions and enables time-resolved studies. In the case of metalloenzymes that are h

Externí odkaz: https://doaj.org/article/288bb78b21864584a71fa98e261fa74e

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Akademický článek

High-throughput structures of protein–ligand complexes at room temperature using serial femtosecond crystallography

Autor: Tadeo Moreno-Chicano, Ali Ebrahim, Danny Axford, Martin V. Appleby, John H. Beale, Amanda K. Chaplin, Helen M. E. Duyvesteyn, Reza A. Ghiladi, Shigeki Owada, Darren A. Sherrell, Richard W. Strange, Hiroshi Sugimoto, Kensuke Tono, Jonathan A. R. Worrall, Robin L. Owen, Michael A. Hough

Publikováno v: IUCrJ, Vol 6, Iss 6, Pp 1074-1085 (2019)

High-throughput X-ray crystal structures of protein–ligand complexes are critical to pharmaceutical drug development. However, cryocooling of crystals and X-ray radiation damage may distort the observed ligand binding. Serial femtosecond crystallog

Externí odkaz: https://doaj.org/article/ad7f2d9a92a74ab3b6301d2289377fb5

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Akademický článek

Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins

Autor: Ali Ebrahim, Tadeo Moreno-Chicano, Martin V. Appleby, Amanda K. Chaplin, John H. Beale, Darren A. Sherrell, Helen M. E. Duyvesteyn, Shigeki Owada, Kensuke Tono, Hiroshi Sugimoto, Richard W. Strange, Jonathan A. R. Worrall, Danny Axford, Robin L. Owen, Michael A. Hough

Publikováno v: IUCrJ, Vol 6, Iss 4, Pp 543-551 (2019)

An approach is demonstrated to obtain, in a sample- and time-efficient manner, multiple dose-resolved crystal structures from room-temperature protein microcrystals using identical fixed-target supports at both synchrotrons and X-ray free-electron la

Externí odkaz: https://doaj.org/article/d85919f46169431f8075520a1390d09b

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Akademický článek

Photoreduction and validation of haem–ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction

Autor: Demet Kekilli, Tadeo Moreno-Chicano, Amanda K. Chaplin, Sam Horrell, Florian S. N. Dworkowski, Jonathan A. R. Worrall, Richard W. Strange, Michael A. Hough

Publikováno v: IUCrJ, Vol 4, Iss 3, Pp 263-270 (2017)

Powerful synergies are available from the combination of multiple methods to study proteins in the crystalline form. Spectroscopies which probe the same region of the crystal from which X-ray crystal structures are determined can give insights into r

Externí odkaz: https://doaj.org/article/8b2bf4548c0b4d05886fcd59e4cd3373

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Three-dimensional structure of the single domain cupredoxin AcoP

Autor: Magali Roger, Philippe Leone, Ninan Blackburn, Sam Horrell, Tadeo Moreno Chicano, Marie-Thérèse Giudici-Orticoni, Luciano A. Abriata, Greg L. Hura, Michael A. Hough, Giulano Sciara, Marianne Ilbert

Cupredoxins are widely occurring copper-binding proteins with a typical Greek-key beta barrel fold. They are generally described as electron carriers that rely on a T1 copper center coordinated by four ligands provided by the folded polypeptide. The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f517401cdf87899953765da01bd9227
https://doi.org/10.1101/2022.03.21.484586

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Structural and functional characterization of the intracellular filament-forming nitrite oxidoreductase multiprotein complex

Autor: Guylaine H. L. Nuijten, Naomi M. de Almeida, Mike S. M. Jetten, Kerstin-Anikó Seifert, Thomas R. M. Barends, Andreas Dietl, Mohd Akram, Joachim Reimann, Tadeo Moreno Chicano, L. Dietrich, Elisabeth Hartmann, Daniel Leopoldus, Laura van Niftrik, F. Leidreiter, Ilme Schlichting, Boran Kartal, Kristian Parey, Melanie Mueller, Ricardo M. Sanchez

Publikováno v: Nature Microbiology, 2021, pp. 1-22
Nature Microbiology
Nature Microbiology, 2021, 1-22

Nitrate is an abundant nutrient and electron acceptor throughout Earth’s biosphere. Virtually all nitrate in nature is produced by the oxidation of nitrite by the nitrite oxidoreductase (NXR) multiprotein complex. NXR is a crucial enzyme in the glo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35f83ade72bb56910288a8acdcf62b2a
https://repository.ubn.ru.nl/handle/2066/235240

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An Aromatic Dyad Motif in Dye Decolourising Peroxidases Has Implications for Free Radical Formation and Catalysis

Autor: Jonathan A. R. Worrall, Michael A. Hough, Tadeo Moreno Chicano, Amanda K. Chaplin, Dimitri A. Svistunenko, Bethany V. Hampshire, Michael T. Wilson

Publikováno v: Chemistry (Weinheim an der Bergstrasse, Germany). 25(24)

Dye decolouring peroxidases (DyPs) are the most recent class of heme peroxidase to be discovered. On reacting with H2 O2 , DyPs form a high-valent iron(IV)-oxo species and a porphyrin radical (Compound I) followed by stepwise oxidation of an organic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74d82075969cc85bfeeb1067ab5785f5
https://pubmed.ncbi.nlm.nih.gov/30945782

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Correction: One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath)

Autor: Hannah R. Adams, Callie Krewson, Jenny E. Vardanega, Sotaro Fujii, Tadeo Moreno-Chicano, Yoshihiro Sambongi, Dimitri Svistunenko, Jordi Paps, Colin R. Andrew, Michael A. Hough

Publikováno v: Chemical Science

Nature is adept at utilising highly similar protein folds to carry out very different functions, yet the mechanisms by which this functional divergence occurs remain poorly characterised. In certain methanotrophic bacteria, two homologous pentacoordi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bbbd74c1297fc7785c154ae5ef01e2f
https://doi.org/10.1039/c9sc90032b

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