TAILIEUCHUNG - Báo cáo khoa học: The role of the Fe-S cluster in the sensory domain of nitrogenase transcriptional activator VnfA from Azotobacter vinelandii

Transcriptional activator VnfA is required for the expression of a second nitrogenase system encoded in thevnfHandvnfDGKoperons inAzotobac-ter vinelandii. In the present study, we have purified full-length VnfA pro-duced inE. colias recombinant proteins (Strep-tag attached and tag-less proteins), enabling detailed characterization of VnfA for the first time. | ỊFEBS Journal The role of the Fe-S cluster in the sensory domain of nitrogenase transcriptional activator VnfA from Azotobacter vinelandii Hiroshi Nakajima1 Nobuyuki Takatani2 Kyohei Yoshimitsu1 Mitsuko Itoh1 Shigetoshi Aono3 Yasuhiro Takahashi4 and Yoshihito Watanabe2 1 Department of Chemistry Graduate Schoolof Science Nagoya University Japan 2 Research Center of Materials Science Nagoya University Japan 3 Okazaki Institute for Integrative Biosciences Japan 4 Division of Life Science Graduate Schoolof Science and Engineering Saitama University Japan Keywords Azotobactor vinelandii iron-sulfur cluster nitrogen fixation nitrogenase transcriptional regulator Correspondence H. Nakajima Department of Chemistry Graduate School of Science Nagoya University Furo-cho Chikusa-ku Nagoya 464-8602 Japan Fax 81 52 789 2953 Tel 81 52 789 3557 E-mail hnakajima@. Database VnfA has been submitted to the Swiss-Prot database under the accession number C1DI41 Received 12 October 2009 revised 28 November 2009 accepted 3 December 2009 doi Transcriptional activator VnfA is required for the expression of a second nitrogenase system encoded in the vnfH and vnfDGK operons in Azotobac-ter vinelandii. In the present study we have purified full-length VnfA produced in E. coli as recombinant proteins Strep-tag attached and tag-less proteins enabling detailed characterization of VnfA for the first time. The EPR spectra of whole cells producing tag-less VnfA VnfA show distinctive signals assignable to a 3Fe-4S cluster in the oxidized form Fe3S4 . Although aerobically purified VnfA shows no vestiges of any Fe-S clusters enzymatic reconstitution under anaerobic conditions reproduced Fe3S4 dominantly in the protein. Additional spectroscopic evidence of Fe3S4 in vitro is provided by anaerobically purified Strep-tag attached VnfA. Thus spectroscopic studies both in vivo and in vitro indicate the involvement of Fe3S4 as a prosthetic group in .

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