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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. Expand
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
- Biology, Medicine
- Nature 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. Expand
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. Expand
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. Expand
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
- Chemistry, Medicine
- 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. Expand
The functioning of the CO2 concentrating mechanism in several cyanobacterial strains: a review of general physiological characteristics, genes, proteins, and recent advances
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... Expand
Influence of leaf dry mass per area, CO2, and irradiance on mesophyll conductance in sclerophylls.
- Foteini Hassiotou, M. Ludwig, M. Renton, E. Veneklaas, John R. Evans
- Biology, Medicine
- Journal 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. Expand
Thioredoxin reductase two modes of catalysis have evolved.
- C. Williams, L. Arscott, +6 authors R. Schirmer
- Medicine, Biology
- European 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. Expand
Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site
- M. Hilgers, M. Ludwig
- Biology, Medicine
- Proceedings 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. Expand
Structure-based perspectives on B12-dependent enzymes.
Two X-ray structures of cobalamin (B12) bound to proteins have now been determined. These structures reveal that the B12 cofactor undergoes a major conformational change on binding to the apoenzymes… Expand