Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Sudipta Shaw"'
Autor:
Fredarla S. Miller, Kathryn K. Crone, Matthew R. Jensen, Sudipta Shaw, William R. Harcombe, Mikael H. Elias, Michael F. Freeman
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Borosins are ribosomally encoded and posttranslationally modified peptide (RiPP) natural products featuring amide-backbone α-N-methylation. Here, the authors report the discovery and characterization of type IV borosin ‘split’ pathways encoding
Externí odkaz:
https://doaj.org/article/09ca9420fa074e35a3fbd77a88dcba46
Autor:
Mikael Elias, Michael F. Freeman, Matthew R. Jensen, William R. Harcombe, Fredarla S. Miller, Sudipta Shaw, Kathryn K. Crone
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
R Code: Supplementary Data 1. Code for running kinetics simulations File name: Supplementary Data 1.R Mass Spectrometry .raw files: Supplementary Figure 4a-c. Mass spectrometric analysis of split borosin coexpressions. File name: 20200110_FSM1167_Son
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44fc191db7bff1230c844edeb083d092
https://pubmed.ncbi.nlm.nih.gov/34504067
https://pubmed.ncbi.nlm.nih.gov/34504067
Autor:
Brian Bothner, Dennis R. Dean, Dmitriy Lukoyanov, Derek F. Harris, Brian M. Hoffman, Philip D. Compton, Lance C. Seefeldt, Monkika Tokmina-Lukaszewska, Sudipta Shaw, Neil L. Kelleher
Publikováno v:
Biochemistry. 57:701-710
Of the three forms of nitrogenase (Mo-nitrogenase, V-nitrogenase, and Fe-nitrogenase), Fe-nitrogenase has the poorest ratio of N2 reduction relative to H2 evolution. Recent work on the Mo-nitrogenase has revealed that reductive elimination of two bri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6885513eb80e410d0921532fd0e0b451
https://doi.org/10.1021/acs.biochem.7b01142
https://doi.org/10.1021/acs.biochem.7b01142
Autor:
Dmitriy Lukoyanov, Dennis R. Dean, Shelley D. Minteer, Nimesh Khadka, Lance C. Seefeldt, Brian M. Hoffman, Sudipta Shaw, Ross D. Milton, Simone Raugei
Publikováno v:
Journal of the American Chemical Society. 139:13518-13524
Nitrogenase catalyzes the reduction of dinitrogen (N2) to two ammonia (NH3) at its active site FeMo-cofactor through a mechanism involving reductive elimination of two [Fe–H–Fe] bridging hydrides to make H2. A competing reaction is the protonatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7724b0cf696417ff3905316a2d152e35
https://doi.org/10.1021/jacs.7b07311
https://doi.org/10.1021/jacs.7b07311
Autor:
Dennis R. Dean, Yanning Zheng, Zhi-Yong Yang, Kathryn R. Fixen, Lance C. Seefeldt, Caroline S. Harwood, Derek F. Harris, Sudipta Shaw
Publikováno v:
Proceedings of the National Academy of Sciences. 113:10163-10167
Nitrogenase is an ATP-requiring enzyme capable of carrying out multielectron reductions of inert molecules. A purified remodeled nitrogenase containing two amino acid substitutions near the site of its FeMo cofactor was recently described as having t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78de780b5786c5671ebbac217805972c
https://doi.org/10.1073/pnas.1611043113
https://doi.org/10.1073/pnas.1611043113
Autor:
Rhesa N. Ledbetter, Dennis R. Dean, Zhi-Yong Yang, Monika Tokmina-Lukaszewska, Valerie L. Cash, Natasha Pence, Brian Bothner, Edwin Antony, Brian J. Eilers, Sudipta Shaw, John W. Peters, Lance C. Seefeldt, Nilisha Pokhrel, Qingjuan Guo
Publikováno v:
Biochemistry. 55:3625-3635
Nitrogenase reduction of dinitrogen (N2) to ammonia (NH3) involves a sequence of events that occur upon the transient association of the reduced Fe protein containing two ATP molecules with the MoFe protein that includes electron transfer, ATP hydrol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b22f6bc6840e8be62b0f2053710dbeea
https://doi.org/10.1021/acs.biochem.6b00421
https://doi.org/10.1021/acs.biochem.6b00421
Autor:
Nimesh, Khadka, Ross D, Milton, Sudipta, Shaw, Dmitriy, Lukoyanov, Dennis R, Dean, Shelley D, Minteer, Simone, Raugei, Brian M, Hoffman, Lance C, Seefeldt
Publikováno v:
Journal of the American Chemical Society. 139(38)
Nitrogenase catalyzes the reduction of dinitrogen (N2) to two ammonia (NH3) at its active site FeMo-cofactor through a mechanism involving reductive elimination of two [Fe-H-Fe] bridging hydrides to make H2. A competing reaction is the protonation of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8ddff1b4d12a4a7438ace9c2b9ff190a
https://pubmed.ncbi.nlm.nih.gov/28851217
https://pubmed.ncbi.nlm.nih.gov/28851217
Autor:
Dmitriy Lukoyanov, Brian M. Hoffman, Lance C. Seefeldt, Sudipta Shaw, Dennis R. Dean, Karamatullah Danyal
Publikováno v:
Journal of the American Chemical Society. 136:12776-12783
Investigations of reduction of nitrite (NO2–) to ammonia (NH3) by nitrogenase indicate a limiting stoichiometry, NO2– + 6e– + 12ATP + 7H+ → NH3 + 2H2O + 12ADP + 12Pi. Two intermediates freeze-trapped during NO2– turnover by nitrogenase vari
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2cc209aa8340483a5f6edbaf5b6e3efe
https://doi.org/10.1021/ja507123d
https://doi.org/10.1021/ja507123d
Autor:
Masaki Horitani, Dennis R. Dean, Edwin Antony, Brian M. Hoffman, Simon Duval, Lance C. Seefeldt, Amy R. Marts, Sudipta Shaw, Simone Raugei, Dmitriy Lukoyanov, Karamatullah Danyal, Taylor R. Page
Publikováno v:
Proceedings of the National Academy of Sciences. 113
Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to two ammonia (NH3) molecules through the participation of its two protein components, the MoFe and Fe proteins. Electron transfer (ET) from the Fe protein to the catalytic MoFe pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::164ab6a3764d3b1e1534486d973dd2e2
https://doi.org/10.1073/pnas.1613089113
https://doi.org/10.1073/pnas.1613089113
Autor:
Sudipta, Shaw, Dmitriy, Lukoyanov, Karamatullah, Danyal, Dennis R, Dean, Brian M, Hoffman, Lance C, Seefeldt
Publikováno v:
Journal of the American Chemical Society
Investigations of reduction of nitrite (NO2(-)) to ammonia (NH3) by nitrogenase indicate a limiting stoichiometry, NO2(-) + 6e(-) + 12ATP + 7H(+) → NH3 + 2H2O + 12ADP + 12Pi. Two intermediates freeze-trapped during NO2(-) turnover by nitrogenase va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3fa39c6f4df4fc6cf9f7b9ea7a6b3b36
https://pubmed.ncbi.nlm.nih.gov/25136926
https://pubmed.ncbi.nlm.nih.gov/25136926