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Title: Light-driven carbon dioxide reduction to methane by nitrogenase in a photosynthetic bacterium

Authors:
; ; ; ; ; ; ; ORCiD logo
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1319953
Grant/Contract Number:
SC0012518
Resource Type:
Journal Article: Published Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Volume: 113; Journal Issue: 36; Related Information: CHORUS Timestamp: 2016-12-23 00:01:35; Journal ID: ISSN 0027-8424
Publisher:
Proceedings of the National Academy of Sciences
Country of Publication:
United States
Language:
English

Citation Formats

Fixen, Kathryn R., Zheng, Yanning, Harris, Derek F., Shaw, Sudipta, Yang, Zhi-Yong, Dean, Dennis R., Seefeldt, Lance C., and Harwood, Caroline S. Light-driven carbon dioxide reduction to methane by nitrogenase in a photosynthetic bacterium. United States: N. p., 2016. Web. doi:10.1073/pnas.1611043113.
Fixen, Kathryn R., Zheng, Yanning, Harris, Derek F., Shaw, Sudipta, Yang, Zhi-Yong, Dean, Dennis R., Seefeldt, Lance C., & Harwood, Caroline S. Light-driven carbon dioxide reduction to methane by nitrogenase in a photosynthetic bacterium. United States. doi:10.1073/pnas.1611043113.
Fixen, Kathryn R., Zheng, Yanning, Harris, Derek F., Shaw, Sudipta, Yang, Zhi-Yong, Dean, Dennis R., Seefeldt, Lance C., and Harwood, Caroline S. 2016. "Light-driven carbon dioxide reduction to methane by nitrogenase in a photosynthetic bacterium". United States. doi:10.1073/pnas.1611043113.
@article{osti_1319953,
title = {Light-driven carbon dioxide reduction to methane by nitrogenase in a photosynthetic bacterium},
author = {Fixen, Kathryn R. and Zheng, Yanning and Harris, Derek F. and Shaw, Sudipta and Yang, Zhi-Yong and Dean, Dennis R. and Seefeldt, Lance C. and Harwood, Caroline S.},
abstractNote = {},
doi = {10.1073/pnas.1611043113},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 36,
volume = 113,
place = {United States},
year = 2016,
month = 8
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1073/pnas.1611043113

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  • Nitrogenase proteins were isolated from cultures of the photosynthetic bacterium Rhodopseudomonas capsulata grown on a limiting amount of ammonia. Under these conditions, the nitrogenase N/sub 2/ase A was active in vivo, and nitrogenase activity in vitro was not dependent upon manganese and the activating factor. The nitrogenase proteins were also isolated from nitrogen-limited cultures in which the in vivo nitrogenase activity had been stopped by an ammonia shock. This nitrogenase activity, N/sub 2/ase R, showed an in vitro requirement for manganese and the activating factor for maximal activity. The Mo-Fe protein (dinitrogenase) was composed of two dissimilar subunits with molecularmore » weights of 55,000 and 59,500; the Fe protein (dinitrogenase reductase), from either type of culture, was composed of a single subunit (molecular weight, 33,500). The metal and acid labile sulfur contents of both nitrogenase proteins were similar to those found for previously isolated nitrogenases. The Fe proteins from both N/sub 2/ase a and N/sub 2/ase R contained phosphate and ribose, 2 mol of each per mol of N/sub 2/ase R Fe protein contained about 1 mol per mol of an adenine-like molecule, whereas the N/sub 2/ase A Fe protein content of this compound was insignificant. These results are compared with various models previously presented for the short-term regulation of nitrogenase activity in the photosynthetic bacteria.« less
  • The addition of NH[sub 4]Cl at concentrations of more than 1 mM completely inhibited nitrogenase-dependent hydrogen evolution using 1 mM succinate as a substrate in the marine photosynthetic bacterium Rhodopseudomonas sp. strain W-1S. However, cells could derepress nitrogenase within 6 h in the presence of NH[sub 4]Cl. The inhibition by 1 mM NH[sub 4]Cl was removed by increasing the concentration of the substrate for hydrogen evolution. The addition of L-methionine-D,L-sulfoximine (MSX), an inhibitor of glutamine synthetase (GS), also removed the inhibition by 1 mM NH[sub 4]Cl. These results indicated that under an argon gas phase, nitrogenase-dependent hydrogen evolution is inhibitedmore » by ATP-consuming GS activity in the presence of NH[sub 4]Cl. The authors isolated a mutant strain, CR-8, which is capable of active hydrogen evolution in the presence of 1 mM NH[sub 4]Cl. 7 refs., 5 figs.« less
  • A thorough review article on work to publication date on the photocatalysis and photoelectrochemistry of CO 2 reduction chemistry. This work also contains an up to date tutorial on photoelectrochemistry in general.