X-ray dose-dependent structural changes of the [2Fe-2S] ferredoxin from Chlamydomonas reinhardtii
- 1 June 2020
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 167 (6), 549-555
- https://doi.org/10.1093/jb/mvaa045
Abstract
Plant-type ferredoxin (Fd) is an electron transfer protein in chloroplast. Redox-dependent structural change of Fd controls its association with and dissociation from Fd-dependent enzymes. Among many X-ray structures of oxidized Fd have been reported so far, very likely a given number of them was partially reduced by strong X-ray. To understand the precise structural change between reduced and oxidized Fd, it is important to know whether the crystals of oxidized Fd may or may not be reduced during the X-ray experiment. We prepared the thin plate-shaped Fd crystals from Chlamydomonas reinhardtii and monitored its absorption spectra during experiment. Absorption spectra of oxidized Fd crystals were clearly changed to that of reduced form in an X-ray dose-dependent manner. In another independent experiment, the X-ray diffraction images obtained from different parts of one single crystal were sorted and merged to form two datasets with low and high X-ray doses. An Fo-Fo map calculated from the two datasets showed that X-ray reduction causes a small displacement of the iron atoms in the [2Fe-2S] cluster. Both our spectroscopic and crystallographic studies confirm X-ray dose-dependent reduction of Fd, and suggest a structural basis for its initial reduction step especially in the core of the cluster.Funding Information
- Ministry of Culture, Education, Science and Sports of Japan (16H06560)
This publication has 26 references indexed in Scilit:
- Dynamics and energetics of cyanobacterial photosystem I:ferredoxin complexes in different redox statesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2017
- X-ray Structure and Nuclear Magnetic Resonance Analysis of the Interaction Sites of the Ga-Substituted Cyanobacterial FerredoxinBiochemistry, 2015
- Increasing the electron-transfer ability of Cyanidioschyzon merolae ferredoxin by a one-point mutation – A high resolution and Fe-SAD phasing crystal structure analysis of the Asp58Asn mutantBiochemical and Biophysical Research Communications, 2013
- Atomic Resolution Structures of Rieske Iron-Sulfur Protein: Role of Hydrogen Bonds in Tuning the Redox Potential of Iron-Sulfur ClustersStructure, 2007
- Structural Basis for the Thermostability of Ferredoxin from the Cyanobacterium Mastigocladus laminosusJournal of Molecular Biology, 2005
- Theoretical Investigation of the “CO in”−“CO out” Isomerization in a [2Fe−2S] Ferredoxin: Free Energy Profiles and Redox StatesJournal of the American Chemical Society, 2003
- An Approach Based on Quantum Chemistry Calculations and Structural Analysis of a [2Fe-2S*] Ferredoxin That Reveal a Redox-Linked Switch in the Electron-Transfer Process to the Fd-NADP+ ReductaseJournal of the American Chemical Society, 2002
- Common and Uncommon Cytochrome P450 Reactions Related to Metabolism and Chemical ToxicityChemical Research in Toxicology, 2001
- The Tertiary Structure of Full-Length Bovine Adrenodoxin Suggests Functional DimersArchives of Biochemistry and Biophysics, 2000
- Refined X-ray Structures of the Oxidized, at 1.3 Å, and Reduced, at 1.17 Å, [2Fe−2S] Ferredoxin from the Cyanobacterium Anabaena PCC7119 Show Redox-Linked Conformational ChangesBiochemistry, 1999