Results 91 to 100 of about 1,564 (203)
Proteins: Structure, Function, and Bioinformatics, EarlyView.ABSTRACT BorF is a short‐chain flavin reductase from a desert soil bacterium that uses NADH to reduce FAD to FADH2, which is used by the tryptophan‐6‐halogenase BorH to chlorinate tryptophan in the biosynthetic pathway of borregomycin A. The X‐ray crystal structure of BorF bound to FAD was solved to 2.37 Å by molecular replacement.
Zheng Ma +3 more
wiley +1 more source
Interaction of ferredoxin and ferredoxin-NADP reductase with thylakoids.
, 1983 Ferredoxin-NADP reductase accounts for about 50% of the NADPH diaphorase activity of spinach leaf homogenates. The enzyme is bound to thylakoid membranes, but can be slowly extracted by aqueous buffers. Ferredoxin-NADP reductase can be extracted from the
Nobili R. L. +5 more
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Proteins: Structure, Function, and Bioinformatics, EarlyView.ABSTRACT Proteins are built from modular domains that serve as fundamental units of structure and evolution. While individual domains have been extensively cataloged, their collective distribution across the lineages of life has remained poorly resolved.
Rui Guo +5 more
wiley +1 more source
Angewandte Chemie, Volume 138, Issue 24, 8 June 2026.Association of the L‐cluster with the nitrogenase assembly proteins NifEN (NifENL) or NifB (NifBL) intrinsically endows these proteins with N2‐reducing activity, enabling in vitro N2‐reduction by NifENL and NifBL when supplied with chemical reductants or photoexcited quantum dots while supporting in vivo N2‐fixation in NifENL‐ and NifENL‐expressing ...
Robert Quechol +4 more
wiley +2 more sources
, 2009 PhDMethionine is one of the seven essential amino-acids for humans and is also used in feed supplements, predominantly for poultry and felines. Thus there is commercial interest in producing this nutrient. The final step in the biological synthesis of
Burton-Smith, Raymond Nathaniel
core
, 2010 Reduced ferredoxin is an intermediate in the methylotrophic and aceticlastic pathway of methanogenesis and donates electrons to membrane-integral proteins, which transfer electrons to the heterodisulfide reductase.
Bender, Gunes +5 more
core +1 more source
Outer‐Sphere Tuning of Synthetic Iron–Sulfur Clusters Within Nanoscale Cage Frameworks
Small, EarlyView.Noncovalent encapsulation of a synthetic iron–sulfur cluster within hydrophobic, naphthalenediimide (NDI)‐paneled cages is shown to lead to dramatic changes in the electronic structure and covalency of the Fe─S core. ABSTRACT As atomic‐scale archetypes for multi‐electron transfer, iron–sulfur clusters are compelling candidates for the design of redox ...
Rupal Baliyan +3 more
wiley +1 more source
Frontiers in Microbiology, 2018 The marine obligate hydrocarbonoclastic bacterium Thalassolituus oleivorans MIL-1 metabolizes a broad range of aliphatic hydrocarbons almost exclusively as carbon and energy sources.
Benjamin H. Gregson +5 more
doaj +1 more source
A cross-linked complex between ferredoxin and ferredoxin-NADP+ reductase
, 1984 The water-soluble carbodiimide, N-ethyl-3-(3-dimethylaminopropyl)carbodiimide was found to effectively cross-link ferredoxin to ferredoxin-NADP+ reductase. The covalent complex has a stoichiometry of 1 mol of ferredoxin per mol of the reductase.
G. Zanetti, A. Aliverti, B. Curti
core
Cuproptosis Inducers in Cancer Therapy: State of the Art and Challenges
The Chemical Record, EarlyView.Cuproptosis is emerging as a distinct copper‐dependent cell death pathway, highlighting copper as a potential metabolic vulnerability in cancer. This review examines how coordination chemistry, redox regulation, and nanomaterial design shape Cu reactivity and therapeutic outcomes.
Chiara Ragusa, Valentina Oliveri
wiley +1 more source