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Biochemistry (Washington)

Print ISSN
0006-2960
Electronic ISSN
1520-4995
Impact factor
3.226
Publisher
ACS
URL
http://pubs.acs.org/journal/bichaw
Usage rank
94
Article count
61025
Free count
1512
Free percentage
0.0247767
PDFs via platforms
Proquest, ACS, Gale, CSA, and Acm

  1. Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis.

    Biochemistry (Washington) 47(17):4955 (2008) PMID 18393449 PMCID PMC3542536

    The flavoprotein quiescin-sulfhydryl oxidase (QSOX) rapidly inserts disulfide bonds into unfolded, reduced proteins with the concomitant reduction of oxygen to hydrogen peroxide. This study reports the first heterologous expression and enzymological characterization of a human QSOX1 isoform. Lik...
  2. Cyanolysis and azidolysis of epoxides by haloalcohol dehalogenase: theoretical study of the reaction mechanism and origins of regioselectivity.

    Biochemistry (Washington) 47(17):4973 (2008) PMID 18393443

    Haloalcohol dehalogenase HheC catalyzes the reversible dehalogenation of vicinal haloalcohols to form epoxides and free halides. In addition, HheC is able to catalyze the irreversible and highly regioselective ring-opening of epoxides with nonhalide nucleophiles, such as CN (-) and N 3 (-). For ...
  3. Inhibitors of the molybdenum cofactor containing 4-hydroxybenzoyl-CoA reductase.

    Biochemistry (Washington) 47(17):4964 (2008) PMID 18393440

    4-Hydroxybenzoyl-CoA reductase (4-HBCR) is a member of the xanthine oxidase (XO) family of molybdenum cofactor containing enzymes and catalyzes the irreversible removal of a phenolic hydroxy group by reduction, yielding benzoyl-CoA and water. In this work the effects of various activity modulati...
  4. Platelet endothelial cell adhesion molecule 1 (PECAM-1) and its interactions with glycosaminoglycans: 2. Biochemical analyses.

    Biochemistry (Washington) 47(17):4863 (2008) PMID 18327914

    Platelet endothelial cell adhesion molecule 1 (PECAM-1) (CD31), a member of the immunoglobulin (Ig) superfamily of cell adhesion molecules with six Ig-like domains, has a range of functions, notably its contributions to leukocyte extravasation during inflammation and in maintaining vascular endo...
  5. Enzyme kinetics and binding studies on inhibitors of MEK protein kinase.

    Biochemistry (Washington) 47(17):5017 (2008) PMID 18393446

    Inhibition of the protein kinase, MEK1, is a potential approach for the treatment of cancer. Inhibitors may act by prevention of activation (PoA), which involves interfering with phosphorylation of nonactivated MEK1 by the upstream kinase, B-RAF. Modulation also may occur by inhibition of cataly...
  6. Charge transfer in the K proton pathway linked to electron transfer to the catalytic site in cytochrome c oxidase.

    Biochemistry (Washington) 47(17):4929 (2008) PMID 18393448

    Cytochrome c oxidase couples electron transfer from cytochrome c to O 2 to proton pumping across the membrane. In the initial part of the reaction of the reduced cytochrome c oxidase with O 2, an electron is transferred from heme a to the catalytic site, parallel to the membrane surface. Even th...
  7. A selenocysteine variant of the human copper chaperone for superoxide dismutase. A Se-XAS probe of cluster composition at the domain 3-domain 3 dimer interface.

    Biochemistry (Washington) 47(17):4916 (2008) PMID 18393442

    We report the semisynthesis of a selenocysteine (Sec) derivative of the human copper chaperone for superoxide dismutase, substituted with Sec at the C-terminal C246 residue. Measurements of hCCS-induced SOD1 activation were used to show that the C-terminal CXC sequence is both necessary and suff...
  8. Role of ribosomal protein L27 in peptidyl transfer.

    Biochemistry (Washington) 47(17):4898 (2008) PMID 18393533

    The current view of ribosomal peptidyl transfer is that the ribosome is a ribozyme and that ribosomal proteins are not involved in catalysis of the chemical reaction. This view is largely based on the first crystal structures of bacterial large ribosomal subunits that did not show any protein co...
  9. Monitoring aromatic picosecond to nanosecond dynamics in proteins via 13C relaxation: expanding perturbation mapping of the rigidifying core mutation, V54A, in eglin c.

    Biochemistry (Washington) 47(17):4876 (2008) PMID 18393447 PMCID PMC3062916

    Long-range effects, such as allostery, have evolved in proteins as a means of regulating function via communication between distal sites. An NMR-based perturbation mapping approach was used to more completely probe the dynamic response of the core mutation V54A in the protein eglin c by monitori...
  10. Cu(II) binding to monomeric, oligomeric, and fibrillar forms of the Alzheimer's disease amyloid-beta peptide.

    Biochemistry (Washington) 47(17):5006 (2008) PMID 18393444

    Copper has been proposed to play a role in Alzheimer's disease through interactions with the amyoid-beta (Abeta) peptide. The coordination environment of bound copper as a function of Cu:Abeta stoichiometry and Abeta oligomerization state are particularly contentious. Using low-temperature elect...