Results 91 to 100 of about 945 (112)

Synthesis and reactivity studies of model complexes for molybdopterin-dependent enzymes

Journal of Inorganic Biochemistry, 2000
The molybdenum cofactor (Moco)-containing enzymes are divided into three classes that are named after prototypical members of each family, viz. sulfite oxidase, DMSO reductase and xanthine oxidase. Functional or structural models have been prepared for these three prototypical enzymes: (i) The complex [MoO2(mnt)2]2- (mnt2- = 1,2 ...
Anders Thapper, Ebbe Nordlander, Christian Lorber   +2 more
exaly   +3 more sources

Synthesis of 1,3-dithiol-2-ones as proligands related to molybdopterin

Organic & Biomolecular Chemistry, 2002
The reaction of suitably disubstituted alkynes with diisopropyl xanthogen disulfide gives differentially substituted 4,5-disubstituted-1,3-dithiol-2-ones as proligands for metal complexes related to the molybdenum cofactor.
Ben, Bradshaw, David, Collison, C David, Garner, John A, Joule   +3 more
openaire   +2 more sources

Designing the Molybdopterin Core through Regioselective Coupling of Building Blocks

Chemistry – A European Journal, 2015
AbstractMolybdopterin is an essential cofactor for all forms of life. The cofactor is composed of a pterin moiety appended to a dithiolene‐functionalized pyran ring, and through the dithiolene moiety it binds metal ions. Different synthetic strategies for dithiolene‐functionalized pyran precursors that have been designed and synthesized are discussed ...
Igor V, Pimkov, Barbara, Serli-Mitasev, Antoinette A, Peterson, Stephen C, Ratvasky, Bernd, Hammann, Partha, Basu   +5 more
openaire   +2 more sources

Molybdopterin--problems and perspectives.

BioFactors (Oxford, England), 1989
Structural studies on several derivatives of molybdopterin, the organic component of the molybdenum cofactor common to virtually all molybdoenzymes, have provided definitive evidence for the presence of a reduced pterin ring with a 6-alkyl side-chain containing an enedithiol and a phosphomonoester in active molybdopterin.
openaire   +1 more source

Molybdenum-maltolate as a molybdopterin mimic for bioinspired oxidation reaction

Dalton Transactions
A novel, non-toxic cis -dioxomolybdenum-maltolate was synthesized as a model molybdopterin mimic for bioinspired oxidation reactions, which shows potential as a micronutrient supplement for molybdenum.
Swapnil S. Pawar, Rohit N. Ketkar, Pranav B. Gaware, Kaustubh U. Jagushte, Divyani Dhawne, Shreyada N. Save, Shilpy Sharma, Ganga Periyasamy, Niyamat Chimthanawala, Sadhana Sathaye, Shreerang V. Joshi, Nabanita Sadhukhan   +11 more
openaire   +2 more sources

BIOSYNTHESIS AND METABOLISM OF TETRAHYDROBIOPTERIN AND MOLYBDOPTERIN

Annual Review of Biochemistry, 1985
C A, Nichol, G K, Smith, D S, Duch
openaire   +3 more sources

‘Molybdopterin’ complexes

Journal of Inorganic Biochemistry, 2003
C.David Garner, Tarnjeet N. Bhachu, Stephen E. Davies, Christopher J. Lowe, Jonathan McMaster, Josephine M. Tunney, James P. Dicks, Ben Bradshaw, David Collison, John A. Joule, Rehana Karim   +10 more
openaire   +1 more source

Identification of molybdopterins in molybdenum- and selenium-containing enzymes.

BioFactors (Oxford, England), 1997
Selenium is coordinated to a molybdenum atom in nicotinic acid hydroxylase (NAH) from Clostridium barkeri and formate dehydrogenase H (FDH) from Escherichia coli. Selenium is present in FDH in a selenocysteine residue whereas in NAH in occurs in an unidentified labile cofactor.
V N, Gladyshev, P, Lecchi
openaire   +1 more source

Molybdopterin

2013
openaire   +2 more sources

Biochemical Aspects of Molybdopterin

1990
K.V. Rajagopalan, Jean L. Johnson, Steven P. Kramer, Michael E. Johnson, Muktimoy Chaudhury, Susan Gardlik, Diana Pitterle, Morgot M. Wuebbens   +7 more
openaire   +1 more source