Results 231 to 240 of about 179,106 (262)

Protein–Protein Complex Formation Affects the Ni–Fe and Fe–S Centers in the H₂‐Sensing Regulatory Hydrogenase from Ralstonia eutropha H16

ChemPhysChem, 2010
AbstractThe regulatory Ni–Fe hydrogenase (RH) from the H2‐oxidizing bacterium Ralstonia eutropha functions as an oxygen‐resistant hydrogen sensor, which is composed of the large, active‐site‐containing HoxC subunit and the small subunit HoxB carrying Fe–S clusters. In vivo, the HoxBC subunits form a dimer designated as RHwt.
Löscher, S., Gebler, A., Stein, M. ; https://orcid.org/0000-0001-7793-0052, Sanganas, O., Buhrke, T., Zebger, I., Dau, H., Friedrich, B., Lenz, O., Haumann, M.   +9 more
openaire   +4 more sources

Chemical and electrochemical interrelationships of the 1-Fe, 2-Fe, and 4-Fe analogs of the active sites of iron-sulfur proteins

Inorganic Chemistry, 1977
Die ein-, zwei- und vier-kernigen Titelkomplexe (I) bis (IV) sind aus einfachen Eisensalzen zuganglich.
J. Cambray, R. W. Lane, A. G. Wedd, Richard W. Johnson, R. H. Holm   +4 more
openaire   +1 more source

Variations on a theme of Fe-O-Fe proteins

Biochemical Society Transactions, 1994
P C, Wilkins, H, Dalton
openaire   +2 more sources

Fe-S Proteins

2021
openaire   +1 more source

Zur Magnetochemie des Systems Fe/Porphyrin/Protein

1964
Temperatur-Gleichgewichte bzwischen“low-spin”-und“high-spin”-Zustanden von d5-Ionen-Komplexen wurden vom Vortragenden 1956 fur das System Fe/Porphyrin/Protein vorausgesagt (1,1a). Sie sind inzwischen gefunden worden (2,3). Die Voraussage solcher Gleichgewichte, die fur relativ kleine Temperaturintervalle im Raumtemperatur-Bereich nur in ganz seltenen ...
openaire   +1 more source

The contemporary management of cancers of the sinonasal tract in adults

Ca-A Cancer Journal for Clinicians, 2023
Rajat Thawani
exaly  

NMR of FeS Proteins

1998
BERTINI, IVANO, LUCHINAT, CLAUDIO, Soriano A.   +2 more
openaire   +2 more sources

PROTAC targeted protein degraders: the past is prologue

Nature Reviews Drug Discovery, 2022
Miklos Bekes, David R Langley, Craig M Crews   +2 more
exaly  

Protein-protein recognition: The neonatal Fe receptor and immunoglobulin G

2001
The neonatal Fe receptor (FeRn) binds the Fe portion of immunoglobulin G (IgG) at the acidic pH of endosomes or the gut and releases IgG at the alkaline pH of blood. FeRn is responsible for the maternofetal transfer of IgG and for rescuing endocytosed IgG from a default degradative pathway.
openaire   +1 more source

Folding/unfolding of FeS proteins

Journal of Inorganic Biochemistry, 1997
I. Bertini, J. Cowan, C. Luchinat, K. Natarajan, M. Piccioli   +4 more
openaire   +1 more source