Zobrazeno 1 - 10
of 181
pro vyhledávání: '"Amy C, Rosenzweig"'
Autor:
Yanan Zhu, Christopher W. Koo, C. Keith Cassidy, Matthew C. Spink, Tao Ni, Laura C. Zanetti-Domingues, Benji Bateman, Marisa L. Martin-Fernandez, Juan Shen, Yuewen Sheng, Yun Song, Zhengyi Yang, Amy C. Rosenzweig, Peijun Zhang
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)
Particulate methane monooxygenase (pMMO) is the main enzyme used by methanotrophs. Here, the authors determined the native structure of pMMO by cryo-electron tomography, revealing lipid-stabilized features and a higher-order hexagonal array arrangeme
Externí odkaz:
https://doaj.org/article/a4c31e824df8458882d3c119c9e2d183
Autor:
Soo Y. Ro, Luis F. Schachner, Christopher W. Koo, Rahul Purohit, Jonathan P. Remis, Grace E. Kenney, Brandon W. Liauw, Paul M. Thomas, Steven M. Patrie, Neil L. Kelleher, Amy C. Rosenzweig
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
The activity of the membrane-bound enzyme pMMO depends on copper but the location of the copper centers is still under debate. Here, the authors reconstitute pMMO in nanodiscs and use native top-down MS to localize its copper centers, providing insig
Externí odkaz:
https://doaj.org/article/7bb55c7a2850428c843bfecc0230d63e
Autor:
Oriana S. Fisher, Grace E. Kenney, Matthew O. Ross, Soo Y. Ro, Betelehem E. Lemma, Sharon Batelu, Paul M. Thomas, Victoria C. Sosnowski, Caroline J. DeHart, Neil L. Kelleher, Timothy L. Stemmler, Brian M. Hoffman, Amy C. Rosenzweig
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Methane- and ammonia-oxidizing bacteria use the integral membrane, copper-dependent enzymes particulate methane monooxygenase (pMMO) and ammonia monooxygenase (AMO) to oxidize methane and ammonia. Here the authors structurally characterize the copper
Externí odkaz:
https://doaj.org/article/743d3e50befe40f495dd9e6768ae3eb0
Autor:
Luis F. Schachner, Benjamin Des Soye, Soo Ro, Grace E. Kenney, Ashley N. Ives, Taojunfeng Su, Young Ah Goo, Michael C. Jewett, Amy C. Rosenzweig, Neil L. Kelleher
Publikováno v:
ACS Chemical Biology. 17:2769-2780
Triosephosphate isomerase (TPI) performs the 5th step in glycolysis, operates near the limit of diffusion, and is involved in "moonlighting" functions. Its dimer was found singly phosphorylated at Ser20 (pSer20) in human cells, with this post-transla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ff0eec866e0579872d32c5d972b763b
https://doi.org/10.1021/acschembio.2c00324
https://doi.org/10.1021/acschembio.2c00324
Autor:
Craig D. Blanchette, Jennifer M. Knipe, Joshuah K. Stolaroff, Joshua R. DeOtte, James S. Oakdale, Amitesh Maiti, Jeremy M. Lenhardt, Sarah Sirajuddin, Amy C. Rosenzweig, Sarah E. Baker
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
There is a need for small-scale reactors that convert methane emissions to more valuable products to reduce climate impacts. Here, the authors show that printing 3D structures of the pMMO enzyme enables continuous methane conversion under ambient con
Externí odkaz:
https://doaj.org/article/69855c700c6243af8d96503a5a0b2b92
Autor:
Anastasia C. Manesis, Jeffrey W. Slater, Kenny Cantave, J. Martin Bollinger, Carsten Krebs, Amy C. Rosenzweig
Publikováno v:
Biochemistry
The diheme bacterial cytochrome c peroxidase (bCcP)/MauG superfamily is a diverse set of enzymes that remains largely uncharacterized. One recently discovered member, MbnH, converts a tryptophan residue in its substrate protein, MbnP, to kynurenine.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6504117da0ffcc2c7714f596410e192d
https://europepmc.org/articles/PMC10083075/
https://europepmc.org/articles/PMC10083075/
Publikováno v:
ACS Synth Biol
Particulate methane monooxygenase (pMMO) is a multi-subunit membrane metalloenzyme used by methanotrophic bacteria to convert methane to methanol. A major hurdle to studying pMMO is the lack of a recombinant expression system, precluding investigatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eba0c78c5f1c94012d5fce37818dfcb5
https://pubmed.ncbi.nlm.nih.gov/36417751
https://pubmed.ncbi.nlm.nih.gov/36417751
Autor:
Rana Montaser, Grace E. Kenney, Neil L. Kelleher, Paul M. Thomas, Yun Ji Park, Amy C. Rosenzweig, Gerri M. Roberts
Publikováno v:
Biochemistry
Methanobactins (Mbns) are ribosomally produced, post-translationally modified peptidic natural products that bind copper with high affinity. Methanotrophic bacteria use Mbns to acquire copper needed for enzymatic methane oxidation. Despite the presen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a42d6bcbeb6ae1069947b8216cd0f0c
https://doi.org/10.1021/acs.biochem.1c00443
https://doi.org/10.1021/acs.biochem.1c00443
Autor:
Peter E. Doan, Amy C. Rosenzweig, Brian M. Hoffman, Christopher W. Koo, Matthew O. Ross, Richard J. Jodts
Publikováno v:
Journal of the American Chemical Society. 143:15358-15368
In nature, methane is oxidized to methanol by two enzymes, the iron-dependent soluble methane monooxygenase (sMMO) and the copper-dependent particulate MMO (pMMO). While sMMO's diiron metal active site is spectroscopically and structurally well-chara
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6221be8aa105ba32baeb5e97b2270b8b
https://doi.org/10.1021/jacs.1c07018
https://doi.org/10.1021/jacs.1c07018
Autor:
Yun Ji Park, Richard J. Jodts, Jeffrey W. Slater, Reyvin M. Reyes, Valerie J. Winton, Rana A. Montaser, Paul M. Thomas, William B. Dowdle, Anahi Ruiz, Neil L. Kelleher, J. Martin Bollinger, Carsten Krebs, Brian M. Hoffman, Amy C. Rosenzweig
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(13)
Significance Methanobactins (Mbns), copper-binding peptidic compounds produced by some bacteria, are candidate therapeutics for human diseases of copper overload. The paired oxazolone-thioamide bidentate ligands of methanobactins are generated from c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf8e01e69ca3a88d50b092392f789ec1
https://pubmed.ncbi.nlm.nih.gov/35320042
https://pubmed.ncbi.nlm.nih.gov/35320042