6aiq
From Proteopedia
High resolution structure of recombinant high-potential iron-sulfur protein
Structural highlights
FunctionHIP_THETI Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. Publication Abstract from PubMedPerdeuteration in neutron crystallography is an effective method for determining the positions of hydrogen atoms in proteins. However, there is shortage of evidence that the high-resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we determined the X-ray structure of perdeuterated high-potential iron-sulfur protein (HiPIP) at a high resolution of 0.85 a resolution. The comparison of the nondeuterated and perdeuterated structures of HiPIP revealed slight differences between the two structures. The spectroscopic and spectroelectrochemical studies also showed that perdeuterated HiPIP has approximately the same characteristics as nondeuterated HiPIP. These results further emphasize the suitability of using perdeuterated proteins in the high-resolution neutron crystallography. Characterization of perdeuterated high-potential iron-sulfur protein with high-resolution X-ray crystallography.,Hanazono Y, Takeda K, Miki K Proteins. 2019 Jul 31. doi: 10.1002/prot.25793. PMID:31365157[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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