Journal Article FZJ-2020-01848

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Visualizing the protons in a metalloenzyme electron proton transfer pathway

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2020
National Acad. of Sciences Washington, DC

Proceedings of the National Academy of Sciences of the United States of America 117(12), 6484 - 6490 () [10.1073/pnas.1918936117]

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Abstract: In redox metalloenzymes, the process of electron transfer often involves the concerted movement of a proton. These processes are referred to as proton-coupled electron transfer, and they underpin a wide variety of biological processes, including respiration, energy conversion, photosynthesis, and metalloenzyme catalysis. The mechanisms of proton delivery are incompletely understood, in part due to an absence of information on exact proton locations and hydrogen bonding structures in a bona fide metalloenzyme proton pathway. Here, we present a 2.1-Å neutron crystal structure of the complex formed between a redox metalloenzyme (ascorbate peroxidase) and its reducing substrate (ascorbate). In the neutron structure of the complex, the protonation states of the electron/proton donor (ascorbate) and all of the residues involved in the electron/proton transfer pathway are directly observed. This information sheds light on possible proton movements during heme-catalyzed oxygen activation, as well as on ascorbate oxidation.

Keyword(s): Health and Life (1st) ; Biology (2nd)

Classification:

Contributing Institute(s):
  1. JCNS-FRM-II (JCNS-FRM-II)
  2. Heinz Maier-Leibnitz Zentrum (MLZ)
  3. Neutronenstreuung (JCNS-1)
Research Program(s):
  1. 6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623) (POF3-623)
  2. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)
  3. 6G15 - FRM II / MLZ (POF3-6G15) (POF3-6G15)
Experiment(s):
  1. BIODIFF: Diffractometer for large unit cells (NL1)

Appears in the scientific report 2020
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Medline ; Embargoed OpenAccess ; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Agriculture, Biology and Environmental Sciences ; Current Contents - Life Sciences ; Ebsco Academic Search ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; National-Konsortium ; PubMed Central ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection ; Zoological Record
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Institute Collections > JCNS > JCNS-FRM-II
Document types > Articles > Journal Article
Institute Collections > JCNS > JCNS-1
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 Record created 2020-04-29, last modified 2021-01-30


Published on 2020-03-09. Available in OpenAccess from 2020-09-09.:
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