In this contribution, we describe the synthesis and covalent attachment of an analogue of the
flavin mononucleotide (FMN) cofactor onto carboxylic functionalities of single-walled carbon …

A new luciferase from V. campbellii (Lux_Vc) was cloned and expressed in Escherichia coli
and purified to homogeneity. Although the amino acid sequences and the catalytic reactions …

We employ replica-exchange molecular dynamics (REMD) and a hybrid ab initio
multiconfigurational quantum mechanics/molecular mechanics (QM/MM) approach to model …

Bacterial luciferase contains an extended 29-residue mobile loop. Movements of this loop
are governed by binding of either flavin mononucleotide (FMNH 2) or polyvalent anions. To …

Bacterial luciferase catalyzes the reaction of FMNH 2, O 2, and a long chain aliphatic
aldehyde, yielding FMN, carboxylic acid, and blue-green light. The most conserved …

Bacterial luciferases (LuxAB) can be readily classed as slow or fast decay luciferases based
on their rates of luminescence decay in a single turnover assay. Luciferases from Vibrio …

The excited state of 4a-hydroxy-4a, 5-dihydroFMN has been postulated to be the emitter in
the bacterial bioluminescence reaction. However, while the bioluminescence quantum yield …

Campylobacter jejuni is highly unusual among bacteria in forming N-linked glycoproteins.
The heptasaccharide produced by its pgl system is attached to protein Asn through its …

Enterobacterial common antigen (ECA) is a polysaccharide found on the outer membrane of
virtually all gram-negative enteric bacteria and consists of three sugars, N-acetyl-d …

The metabolic pathway for histidine biosynthesis is interesting from an evolutionary
perspective because of the diversity of gene organizations and protein structures involved …