Fe-S Cluster Enzymes Part B

Nonfiction, Science & Nature, Science, Biological Sciences, Cytology, Other Sciences, Molecular Biology
Cover of the book Fe-S Cluster Enzymes Part B by Sheila S. David, Elsevier Science
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Author: Sheila S. David ISBN: 9780128147184
Publisher: Elsevier Science Publication: January 20, 2018
Imprint: Academic Press Language: English
Author: Sheila S. David
ISBN: 9780128147184
Publisher: Elsevier Science
Publication: January 20, 2018
Imprint: Academic Press
Language: English
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Methods in Enzymology, Volume 599 is the second of two volumes focused on Fe-S cluster enzymes. Topics of interest in this new release include steps towards understanding mitochondrial Fe/S cluster biogenesis, iron sulfur clusters in zinc finger proteins, electrochemistry of Iron-sulfur enzymes, NRVS for Fe in biology and its experiment and basic interpretation,

methods for studying iron regulatory protein 1, an important protein in human iron metabolism, the characterization of glutaredoxin Fe-S cluster binding interactions using circular dichroism spectroscopy, fluorescent reporters to track Fe-S cluster assembly and transfer reactions, methods for studying the Fe-S cluster containing base excision repair glycosylase MUTYH, and more.

  • Contain contributions from leading authorities on enzymology
  • Informs and updates on all the latest developments in the field
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Methods in Enzymology, Volume 599 is the second of two volumes focused on Fe-S cluster enzymes. Topics of interest in this new release include steps towards understanding mitochondrial Fe/S cluster biogenesis, iron sulfur clusters in zinc finger proteins, electrochemistry of Iron-sulfur enzymes, NRVS for Fe in biology and its experiment and basic interpretation,

methods for studying iron regulatory protein 1, an important protein in human iron metabolism, the characterization of glutaredoxin Fe-S cluster binding interactions using circular dichroism spectroscopy, fluorescent reporters to track Fe-S cluster assembly and transfer reactions, methods for studying the Fe-S cluster containing base excision repair glycosylase MUTYH, and more.

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