X-ray crystal structure of the light-independent protochlorophyllide reductase

@article{Muraki2010XrayCS,
  title={X-ray crystal structure of the light-independent protochlorophyllide reductase},
  author={N. Muraki and Jiro Nomata and Kozue Ebata and T. Mizoguchi and T. Shiba and H. Tamiaki and G. Kurisu and Y. Fujita},
  journal={Nature},
  year={2010},
  volume={465},
  pages={110-114}
}
Photosynthetic organisms adopt two different strategies for the reduction of the C17 = C18 double bond of protochlorophyllide (Pchlide) to form chlorophyllide a, the direct precursor of chlorophyll a (refs 1–4). The first involves the activity of the light-dependent Pchlide oxidoreductase, and the second involves the light-independent (dark-operative) Pchlide oxidoreductase (DPOR). DPOR is a nitrogenase-like enzyme consisting of two components, L-protein (a BchL dimer) and NB-protein (a BchN… Expand
Crystal Structure of Dark-Operative Protochlorophyllide Reductase Reveals the Structural Basis for Nitrogenase-Like Enzymes
Dark-operative protochlorophyllide reductase (DPOR) catalyses the reduction of protochlorophyllide (Pchlide) to chlorophyllide a, which is a key step in the chlorophyll biosynthesis pathway. DPOR isExpand
Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase
TLDR
Two structures of cyanobacterial LPOR bound to NADPH are reported, which reveals the molecular basis of a NADPH-binding pocket, a substrate cavity, and the proton-relay path, and provide a basis for understanding the structure-function relationships of the light-driven Pchlide reduction. Expand
Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex
TLDR
This study uses protein structure modelling, molecular dynamics simulations, multi-wavelength analytical ultracentrifugation and small angle X-ray scattering experiments to derive a consensus model of the LPOR apoprotein and the substrate/cofactor/LPOR ternary complex, finding that the protein is monomeric in its apo form but that substrate and co-factor binding results in dimerization via the active site surface patch. Expand
Structural and functional studies of the light-dependent protochlorophyllide oxidoreductase enzyme
The light dependent enzyme protochlorophyllide oxidoreductase (POR) is a key enzyme in the chlorophyll biosynthesis pathway, catalysing the reduction of the C17 C18 bond in protochlorophyllideExpand
Stoichiometry of ATP hydrolysis and chlorophyllide formation of dark-operative protochlorophyllide oxidoreductase from Rhodobacter capsulatus.
TLDR
The stoichiometry of ATP hydrolysis and the Chlide formation of DPOR is determined and it is suggested that DPOR has a specific intrinsic property, while retaining the common features shared with nitrogenase. Expand
Structure of ADP-aluminium fluoride-stabilized protochlorophyllide oxidoreductase complex
TLDR
The catalytic differences and similarities between DPOR and nitrogenase have broad implications for the energy transduction mechanism of related multiprotein complexes that are involved in the reduction of chemically stable double and/or triple bonds. Expand
Substrate recognition induces sequential electron transfer across subunits in the nitrogenase-like DPOR complex
TLDR
Allosteric communication between the two identical active sites in Rhodobacter sphaeroides BchNB that drives sequential and asymmetric ET is described, shedding light on the functional advantages imparted by the oligomeric architecture found in many electron transfer enzymes. Expand
Dark-operative protochlorophyllide oxidoreductase generates substrate radicals by an iron-sulphur cluster in bacteriochlorophyll biosynthesis
TLDR
DPOR is a unique iron-sulphur enzyme to form substrate radicals followed by sequential proton- and electron-transfer steps with the protein folding very similar to that of nitrogenase, which supports the biosynthesis of Chl in a wide variety of photosynthetic organisms. Expand
Elucidation of ligand binding and dimerization of NADPH:protochlorophyllide (Pchlide) oxidoreductase from pea (Pisum sativum L.) by structural analysis and simulations
TLDR
Analyzing the sequence and structural relationships among homologous proteins identified through database searches suggests that fit-inducing processes play important roles in POR-Pchlide interactions, and highlights the complexity of interactions of porphyrin-containing ligands with proteins. Expand
Reduction of Chemically Stable Multibonds: Nitrogenase-Like Biosynthesis of Tetrapyrroles.
TLDR
The present working hypothesis mirrors a DPOR and COR related enzyme mechanism of NflH/NflD, and nfl-encoded proteins were suggested as "simplified" ancestors lying basal in the phylogenetic tree between nitrogenase and DPOR/COR. Expand
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References

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Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase with MgADP bound: a homologue of the nitrogenase Fe protein.
TLDR
The newly determined structure of BchL and its comparison to its close homologue, the nitrogenase Fe protein, provide the basis for understanding how these highly related proteins can discriminate between their respective functions in microbial systems where each must function simultaneously. Expand
Reconstitution of Light-independent Protochlorophyllide Reductase from Purified Bchl and BchN-BchB Subunits
TLDR
The first reproducible demonstration of dark protochlorophyllide reductase activity from purified protein subunits that were isolated from the purple nonsulfur photosynthetic bacterium Rhodobacter capsulatus is reported. Expand
Overexpression and characterization of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus.
TLDR
An overexpression system of two separable components of DPOR, L-protein and NB-protein, in the broad-host-range vector pJRD215 in Rhodobacter capsulatus is constructed, providing a framework for the characterization of these components in detail, and further support a nitrogenase model ofDPOR. Expand
ATP-driven Reduction by Dark-operative Protochlorophyllide Oxidoreductase from Chlorobium tepidum Mechanistically Resembles Nitrogenase Catalysis*
TLDR
The heterologous overproduction of DPOR subunits BchN, BchB, and BchL from Chlorobium tepidum in Escherichia coli allowing their purification to apparent homogeneity is described and an enzymatic mechanism ofDPOR is proposed. Expand
Photoprotective role of NADPH:protochlorophyllide oxidoreductase A
TLDR
A homology model of NADPH:protochlorophyllide (Pchlide) oxidoreductase A (POR) of barley is developed and verified by site-directed mutagenesis, providing a photoprotective role of PORA during greening. Expand
A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: identification and mutagenesis of two conserved residues that are essential for enzyme activity.
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TLDR
A model of the enzyme reaction mechanism for light-dependent protochlorophyllide reduction is proposed and two conserved residues are identified and mutated within the proposed active site of the enzymes and shown that they are critical for activity. Expand
Functional expression of nitrogenase-like protochlorophyllide reductase from Rhodobacter capsulatus in Escherichia coli.
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TLDR
These E. coli strains provide a promising system for structural and kinetic analyses of the nitrogenase-like enzymes, and two overexpression plasmids for L-protein and NB-protein were constructed. Expand
Protochlorophyllide oxidoreductase B-catalyzed protochlorophyllide photoreduction in vitro: insight into the mechanism of chlorophyll formation in light-adapted plants.
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TLDR
The PORb-catalyzed reaction in vitro is spectroscopically similar to that identified in leaves of light-adapted plants, suggesting that the same reaction sequence observed operates in planta. Expand
Novel Insights into the Enzymology, Regulation and Physiological Functions of Light-dependent Protochlorophyllide Oxidoreductase in Angiosperms
TLDR
This review provides a brief overview of DPOR, its light-dependent catalytic activity, accumulation in plastids of dark-grown angiosperms (etioplasts) and cofactor, NADPH, resulting in the formation of prolamellar bodies (PLBs), and rapid degradation after catalysis under subsequent illumination. Expand
Evolution of Chlorophyll Biosynthesis—The Challenge to Survive Photooxidation
The capability to perform protochlorophyllide reduction under aerobic conditions and thereby to avoid the danger of photooxidation was certainly a landmark in the evolution of porphyrin biosynthesis.Expand
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