Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Krithika Ganesan"'
Autor:
Sangeeth Krishnan, Maya M.G, Akhil Das, Suja Bhargavan, Krithika Ganesan, Swaminathan Sivaram, Prabha Vadivelu, Lakshminarayanan Ragupathy
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-12 (2022)
Abstract Herein, we report various physico-chemical approaches to probe the nature of the interface between few layers graphene (FLG) and carboxylated nitrile rubber (XNBR) nanocomposites prepared through efficient blending of XNBR latex with an aque
Externí odkaz:
https://doaj.org/article/58c91cfe7ab94be88d3daf79132a2780
Autor:
Prabha Vadivelu, Krithika Ganesan
Publikováno v:
Inorganic Chemistry. 61:19463-19474
Publikováno v:
Inorganic Chemistry. 60:13615-13625
The reactivities of [Mn(13-TMC)(OOH)]2+ (1) and [Mn(13-TMC)(O2)]+ (2) in the sulfoxidation of thioanisole have been compared using density functional theory methods. The orientation of the 13-TMC ligand and substrate and non-redox metal ion effects h
Publikováno v:
Inorganic chemistry. 60(17)
The reactivities of [Mn(13-TMC)(OOH)]
Autor:
Krithika Ganesan, Robert B. Gennis
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1797:619-624
The K-pathway is one of the two proton-input channels required for function of cytochrome c oxidase. In the Rhodobacter sphaeroides cytochrome c oxidase, the K-channel starts at Glu101 in subunit II, which is at the surface of the protein exposed to
Autor:
Krithika Ganesan, Pierre Moënne-Loccoz, Robert B. Gennis, Takahiro Hayashi, James A. Fee, Myat T. Lin, Ying Chen
Publikováno v:
Biochemistry. 48:883-890
Bacterial heme−copper terminal oxidases react quickly with NO to form a heme−nitrosyl complex, which, in some of these enzymes, can further react with a second NO molecule to produce N2O. Previously, we characterized the heme a3−NO complex form
Autor:
Robert B. Gennis, D. Robinson, Neil L. Kelleher, Krithika Ganesan, Todd J. Martínez, James Hemp
Publikováno v:
Biochemistry. 45:15405-15410
In the respiratory chains of aerobic organisms, oxygen reductase members of the heme-copper superfamily couple the reduction of O2 to proton pumping, generating an electrochemical gradient. There are three distinct families of heme-copper oxygen redu
Autor:
Laura A. Pace, Fevzi Daldal, Robert B. Gennis, Krithika Ganesan, Steven R. Blanke, Huazhi Han, Jung Hyeob Roh, James Hemp, Hanlin Ouyang
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24f3bd56bc9295a76cf43293a2ff40fd
https://europepmc.org/articles/PMC3356604/
https://europepmc.org/articles/PMC3356604/
Autor:
Laura A. Pace, Steven R. Blanke, James Hemp, Fevzi Daldal, Huazhi Han, Robert B. Gennis, Krithika Ganesan, Hanlin Ouyang, Jung Hyeob Roh
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 108(34)
Aerobic respiration in bacteria, Archaea, and mitochondria is performed by oxygen reductase members of the heme-copper oxidoreductase superfamily. These enzymes are redox-driven proton pumps which conserve part of the free energy released from oxygen
Autor:
Takahiro, Hayashi, Myat T, Lin, Krithika, Ganesan, Ying, Chen, James A, Fee, Robert B, Gennis, Pierre, Moënne-Loccoz
Publikováno v:
Biochemistry. 48(5)
Bacterial heme-copper terminal oxidases react quickly with NO to form a heme-nitrosyl complex, which, in some of these enzymes, can further react with a second NO molecule to produce N(2)O. Previously, we characterized the heme a(3)-NO complex formed