Nitrogenases catalyze dinitrogen (N) fixation to ammonia (NH). While these enzymes are highly sensitive to deactivation by molecular oxygen (O) they can be produced by obligate aerobes for diazotrophy, necessitating a mechanism by which nitrogenase can be protected from deactivation. In the bacterium Azotobacter vinelandii, one mode of such protection involves an O-responsive ferredoxin-type protein ("Shethna protein II", or "FeSII") which is thought to bind with Mo-dependent nitrogenase's two component proteins (NifH and NifDK) to form a catalytically stalled yet O-tolerant tripartite protein complex.
View Article and Find Full Text PDFThe biological N-fixation process is catalyzed exclusively by metallocofactor-containing nitrogenases. Structural and spectroscopic studies highlighted the presence of an additional mononuclear metal-binding (MMB) site, which can coordinate Fe in addition to the two metallocofactors required for the reaction. This MMB site is located 15-Å from the active site, at the interface of two NifK subunits.
View Article and Find Full Text PDFThe substrate-reducing proteins of all nitrogenases (MoFe, VFe, and FeFe) are organized as αß(γ) multimers with two functional halves. While their dimeric organization could afford improved structural stability of nitrogenases , previous research has proposed both negative and positive cooperativity contributions with respect to enzymatic activity. Here, a 1.
View Article and Find Full Text PDFObjective: We reviewed the mechanism of injury, presentation, and evaluation of children with trauma to the lateral oropharynx. Study design and setting We conducted a retrospective review of patients in an urban pediatric emergency department with trauma to the lateral oropharynx over a 5-year period.
Results: Forty-eight patients were identified with documented injuries of the lateral oropharynx placing the internal carotid artery at risk of injury.