Share This Author
THE DIVERSITY AND COEVOLUTION OF RUBISCO, PLASTIDS, PYRENOIDS, AND CHLOROPLAST-BASED CO2-CONCENTRATING MECHANISMS IN ALGAE
This review examines the potential diversity of both Rubisco and chloroplast-based CCMs across algal divisions, including both green and nongreen algae, and seeks to highlight recent advances in the understanding of the area and future areas for research.
The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia
- B. Guenther, C. Sheppard, P. Tran, R. Rozen, R. Matthews, M. Ludwig
- BiologyNature Structural Biology
Folate derivatives protect wild-type and mutant E. coli enzymes against flavin loss, and protect human MTHFR and the A222V mutant against thermal inactivation, suggesting a mechanism by which folate treatment reduces homocysteine levels.
Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase.
The structure of the flavin-reducing conformation of E. coli TrxR is described and it is demonstrated that switching between the two conformations involves a "ball-and-socket" motion in which the pyridine nucleotide-binding domain rotates by 67 degrees.
One thousand plant transcriptomes and the phylogenomics of green plants
- James H. Michael S. Eric J. Michael K. Matthew A. Sean W Leebens-Mack Barker Carpenter Deyholos Gitzendanne, J. Leebens-Mack, G. Wong
- Biology, Environmental ScienceNature
- 7 October 2019
It is found that large expansions of gene families preceded the origins of green plants, land plants and vascular plants, whereas whole-genome duplications are inferred to have occurred repeatedly throughout the evolution of flowering plants and ferns.
The functioning of the CO2 concentrating mechanism in several cyanobacterial strains: a review of general physiological characteristics, genes, proteins, and recent advances
- G. Price, D. Sültemeyer, B. Klughammer, M. Ludwig, M. Badger
- Environmental Science, Biology
- 1 June 1998
Comparative aspects of physiology, genetics, and proteins involved in the cyanobacterial CCM with particular focus on recent advances are covered, namely Synechocystis PCC6803 (freshwater strain; for which a full genome database is now available),Synechococcus PCC7002 (coastal marine st...
Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S].
Structural and sequence similarities assign PDR to a distinct family of flavoprotein reductases, all related to ferredoxin NADP(+)-reductase, many of which are related to plant ferredoxins.
Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus.
- M. Lah, M. M. Dixon, K. Pattridge, W. Stallings, J. Fee, M. Ludwig
- 7 February 1995
A reaction scheme in which the ligated solvent acts as a proton acceptor in the first half-reaction [formation of Fe(II) and oxygen] is consistent with the pH dependence of the kinetic parameters and spectroscopic properties of Fe superoxide dismutase.
Influence of leaf dry mass per area, CO2, and irradiance on mesophyll conductance in sclerophylls.
- Foteini Hassiotou, M. Ludwig, M. Renton, E. Veneklaas, J. R. Evans
- Environmental ScienceJournal of experimental botany
- 1 May 2009
In this study, laboratory measurements of leaf gas exchange and in vivo chlorophyll a fluorescence were used concurrently to derive estimates of g(m) in seven species of the Australian sclerophyllous genus Banksia covering a wide range of LMA, and a significant decrease of g (m) with increasing LMA was found.
Thioredoxin reductase two modes of catalysis have evolved.
- C. Williams, L. Arscott, R. Schirmer
- Biology, ChemistryEuropean journal of biochemistry
- 1 October 2000
It is hoped that the chemical difference between the two high Mr forms of thioredoxin reductase may be exploited for drug design.
Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site
- M. Hilgers, M. Ludwig
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 11 September 2001
Although the nature of the autoinducer synthesized by LuxS cannot be deduced from the crystal structure, features of the putative active site suggest that LuxS might catalyze hydrolytic, but not proteolytic, cleavage of a small substrate.