Zobrazeno 1 - 10
of 27
pro vyhledávání: '"K. Kristoffer Andersson"'
Importance of Val567 on heme environment and substrate recognition of neuronal nitric oxide synthase
Autor:
Inger K. Olsbu, Giorgio Zoppellaro, K. Kristoffer Andersson, Jean‐Luc Boucher, Hans‐Petter Hersleth
Publikováno v:
FEBS Open Bio, Vol 8, Iss 9, Pp 1553-1566 (2018)
Nitric oxide (NO) produced by mammalian nitric oxide synthases (mNOSs) is an important mediator in a variety of physiological functions. Crystal structures of mNOSs have shown strong conservation of the active‐site residue Val567 (numbering for rat
Externí odkaz:
https://doaj.org/article/027c1482589c4560aff066499dec669e
Publikováno v:
PLoS ONE, Vol 8, Iss 8 (2013)
Externí odkaz:
https://doaj.org/article/2726d581583a470d85ba238d60e7b3af
Autor:
Ane B. Tomter, Giorgio Zoppellaro, Caleb B. Bell, Anne-Laure Barra, Niels H. Andersen, Edward I. Solomon, K. Kristoffer Andersson
Publikováno v:
PLoS ONE, Vol 7, Iss 6 (2012)
Externí odkaz:
https://doaj.org/article/48716c4470784260b6837e161da9105d
Publikováno v:
PLoS ONE, Vol 8, Iss 7, p e69411 (2013)
Thioredoxin-like proteins contain a characteristic C-x-x-C active site motif and are involved in a large number of biological processes ranging from electron transfer, cellular redox level maintenance, and regulation of cellular processes. The mechan
Externí odkaz:
https://doaj.org/article/dfe44617bb0d44f1817a2df9e1cf7a7c
Autor:
Ane B Tomter, Giorgio Zoppellaro, Caleb B Bell, Anne-Laure Barra, Niels H Andersen, Edward I Solomon, K Kristoffer Andersson
Publikováno v:
PLoS ONE, Vol 7, Iss 3, p e33436 (2012)
Ribonucleotide reductase (RNR) catalyzes the rate limiting step in DNA synthesis where ribonucleotides are reduced to the corresponding deoxyribonucleotides. Class Ib RNRs consist of two homodimeric subunits: R1E, which houses the active site; and R2
Externí odkaz:
https://doaj.org/article/154cc23f8ee94fbca899e78116e34c3f
The Methylococcus capsulatus (Bath) secreted protein, MopE*, binds both reduced and oxidized copper.
Autor:
Thomas Ve, Karina Mathisen, Ronny Helland, Odd A Karlsen, Anne Fjellbirkeland, Åsmund K Røhr, K Kristoffer Andersson, Rolf-Birger Pedersen, Johan R Lillehaug, Harald B Jensen
Publikováno v:
PLoS ONE, Vol 7, Iss 8, p e43146 (2012)
Under copper limiting growth conditions the methanotrophic bacterium Methylococcus capsulatus (Bath) secrets essentially only one protein, MopE*, to the medium. MopE* is a copper-binding protein whose structure has been determined by X-ray crystallog
Externí odkaz:
https://doaj.org/article/f1eb7d75ef9146b8a6e2a5ea03fda97c
Autor:
Espen Harbitz, K Kristoffer Andersson
Publikováno v:
PLoS ONE, Vol 6, Iss 7, p e22014 (2011)
A small soluble cytochrome c-554 purified from Methylosinus trichosporium OB3b has been purified and analyzed by amino acid sequencing, mass spectrometry, visible, CD and EPR spectroscopies. It is found to be a mono heme protein with a characteristic
Externí odkaz:
https://doaj.org/article/76b818184fef4ae7b6ada87eb4cb6489
Autor:
Annette, Fagerlund, Veronika, Smith, Åsmund K, Røhr, Toril, Lindbäck, Marthe P, Parmer, K Kristoffer, Andersson, Leon, Reubsaet, Ole Andreas, Økstad
Publikováno v:
Molecular microbiology. 101(3)
Biofilm formation can be considered a bacterial virulence mechanism. In a range of Gram-negatives, increased levels of the second messenger cyclic diguanylate (c-di-GMP) promotes biofilm formation and reduces motility. Other bacterial processes known
Autor:
K. Kristoffer Andersson, Kara L. Bren, Giorgio Zoppellaro, Ravinder Kaur, Espen Harbitz, Amy A. Ensign
Publikováno v:
Journal of the American Chemical Society. 130:15348-15360
Cytochromes of the c type with histidine−methionine (His-Met) heme axial ligation play important roles in electron-transfer reactions and in enzymes. In this work, two series of cytochrome c mutants derived from Pseudomonas aeruginosa (Pa c-551) an
Autor:
Astrid Gräslund, Pieter J. van Dam, Stephan Pötsch, Anne Laure Barra, K. Kristoffer Andersson, Peter P. Schmidt, Brian M. Hoffman, Jean Paul Willems, Wilfred R. Hagen
Publikováno v:
Journal of the American Chemical Society. 120:5080-5085
The g tensor of the tyrosyl radical present in the active R2 protein of ribonucleotide reductase is anisotropic, and the g1 component is influenced by hydrogen bonding to the oxygen of the tyrosyl ...