Results 61 to 70 of about 36,091 (300)
Generating site saturation mutagenesis libraries and transferring them to broad host range plasmids using type IIS restriction enzymes [PDF]
arXiv, 2023 Protein engineering is an established method for tailoring enzymatic reactivity. A commonly used method is directed evolution, where the mutagenesis and natural selection process is mimicked and accelerated in the laboratory. Here, we describe a reliable method for generating saturation mutagenesis libraries by golden gate cloning in a broad host range
arxiv
Test of Host Sanction Hypothesis in Soybean Plants Co-inoculated with Nitrogen Fixing and Non-fixing Bradyrhizobium japonicum [PDF]
, 2015 Aims: We tested the proposed mechanism for potential sanctions, that the plant would reduce viability of non-fixing rhizobia inside nodules, performing viable Bradyrhizobium japonicum counts from co-occupied and single-occupied nodules in co-inoculated ...
Bedmar, Eulogio +2 more
core +1 more source
The electronic complexity of the ground-state of the FeMo cofactor of nitrogenase as relevant to quantum simulations [PDF]
, 2018 We report that a recent active space model of the nitrogenase FeMo cofactor, proposed in the context of quantum simulations, is not representative of the electronic structure of the FeMo cofactor ground-state. Although quantum resource estimates, outside of the cost of adiabatic state preparation, will not be much affected, conclusions should not be ...
arxiv +1 more source
Biosynthesis of Nitrogenase Metalloclusters [PDF]
Chemical Reviews, 2013 Nitrogenase is a complex metalloenzyme that is best known for its function in biological nitrogen fixation.1,2 Harbored in a group of microbes called diazotrophs, nitrogenase catalyzes the reduction of nitrogen (N2) to ammonia (NH3) in a reaction that is usually depicted as N2 + 8H+ + 16MgATP + 8e− → 2NH3 + H2 + 16MgADP + 16Pi.
Keith O. Hodgson +3 more
openaire +3 more sources
Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifB. [PDF]
, 2020 NifB is a radical S-adenosyl-L-methionine (SAM) enzyme that is essential for nitrogenase cofactor assembly. Previously, a nitrogen ligand was shown to be involved in coupling a pair of [Fe4S4] clusters (designated K1 and K2) concomitant with carbide ...
Britt, R David +7 more
core +1 more source
Great metalloclusters in enzymology [PDF]
, 2002 Metallocluster-containing enzymes catalyze some of the most basic redox transformations in the biosphere. The reactions catalyzed by these enzymes typically involve small molecules such as N2, CO, and H2 that are used to generate both chemical building ...
Rees, Douglas C.
core +1 more source
Covalent Organic Frameworks for Photocatalysis
Advanced Materials, EarlyView.This review provides an overview of recent advances in covalent organic frameworks (COFs) for photocatalysis, focusing on sustainable energy applications like water splitting, hydrogen peroxide generation, and CO2 and N2 reduction. It discusses design principles, structure‐function relationships, challenges in COF photocatalysis, and strategies to ...
Bikash Mishra +6 more
wiley +1 more source
Diverse syntrophic partnerships from deep-sea methane vents revealed by direct cell capture and metagenomics [PDF]
, 2008 Microorganisms play a fundamental role in the cycling of nutrients and energy on our planet. A common strategy for many microorganisms mediating biogeochemical cycles in anoxic environments is syntrophy, frequently necessitating close spatial proximity ...
A. E. Dekas +29 more
core +4 more sources
Advanced Science, EarlyView.This study develops a photosynthetic bioelectrochemical nitrogen fixation system for simultaneous nitrogen fixation and current generation using Rhodopseudomonas palustris. Notably, extracellular electron transfer (EET) serves as a redox balancing strategy, suppressing nitrogen fixation by competing with nitrogenase for electrons.
Xuewen Liu +6 more
wiley +1 more source
Biosynthesis of nitrogenase FeMoco [PDF]
Coordination Chemistry Reviews, 2011 Biosynthesis of nitrogenase FeMoco is a highly complex process that requires, minimally, the participation of nifS, nifU, nifB, nifE, nifN, nifV, nifH, nifD and nifK gene products. Previous genetic analyses have identified the essential factors for the assembly of FeMoco; however, the exact functions of these factors and the precise sequence of events ...
Markus W. Ribbe, Yilin Hu
openaire +3 more sources