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Walker, C.J.; Weinstein, J.D.: In vitro assay of the chlorophyll biosynthetic enzyme Mg-chelatase: resolution of the activity into soluble and membrane-bound fractions. Proc. Natl. Acad. Sci. USA, 88, 5789–5793 (1991)
Walker, C.J.; Willows, R.D.: Mechanism and regulation of Mg-chelatase. Biochem. J., 327, 321–333 (1997)
Fodje, M.N.; Hansson, A.; Hansson, M.; Olsen, J.G.; Gough, S.; Willows, R.D.; Al-Karadaghi, S.: Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase. J. Mol. Biol., 311, 111–122 (2001)
Nakayama, M.; Masuda, T.; Sato, N.; Yamagata, H.; Bowler, C.; Ohta, H.; Shioi, Y.; Takamiya, K.: Cloning, subcellular localization and expression of CHL1, a subunit of magnesium-chelatase in soybean. Biochem. Biophys. Res. Commun., 215, 422–428 (1995)
Gorchein, A.: Cell-free activity of magnesium chelatase in Rhodobacter spheroides and Rhodobacter capsulatus. Biochem. Soc. Trans., 25, 82S (1997)
Reid, J.D.; Hunter, C.N.: Current understanding of the function of magnesium chelatase. Biochem. Soc. Trans., 30, 643–645 (2002)
Papenbrock, J.; Mock, H.-P.; Kruse, E.; Grimm, B.: Expression studies in tetrapyrrole biosynthesis: inverse maxima of magnesium chelatase and ferrochelatase activity during cyclic photoperiods. Planta, 208, 264–273 (1999)
Grafe, S.; Saluz, H.-P.; Grimm, B.; Hanel, F.: Mg-chelatase of tobacco: the role of the subunit CHL D in the chelation step of protoporphyrin IX. Proc. Natl. Acad. Sci. USA, 96, 1941–1946 (1999)
Hansson, A.; Willows, R.D.; Roberts, T.H.; Hansson, M.: Three semidominant barley mutants with single amino acid substitutions in the smallest magnesium chelatase subunit form defective AAA+ hexamers. Proc. Natl. Acad. Sci. USA, 99, 13944–13949 (2002)
Willows, R.D.; Lake, V.; Roberts, T.H.; Beale, S.I.: Inactivation of Mg chelatase during transition from anaerobic to aerobic growth in Rhodobacter capsulatus. J. Bacteriol., 185, 3249–3258 (2003)
Yaronskaya, E.B.; Rassadina, V.V.; Averina, N.G.: Regulation of magnesium chelatase activity during excessive accumulation of porphyrins in green barley leaves. Russ. J. Plant Physiol., 49, 771–775 (2002)
Petersen, B.L.; Jensen, P.E.; Gibson, L.C.D.; Stummann, B.M.; Hunter, C.N.; Henningsen, K.W.: Reconstitution of an active magnesium chelatase enzyme complex from the bchI,-D, and-H gene products of the green sulfur bacterium Chlorobium vibrioforme expressed in Escherichia coli. J. Bacteriol., 180, 699–704 (1998)
Karger, G.A.; Reid, J.D.; Hunter, C.N.: Characterization of the binding of deuteroporphyrin IX to the magnesium chelatase H subunit and spectroscopic properties of the complex. Biochemistry, 40, 9291–9299 (2001)
Jensen, P.E.; Reid, J.D.; Hunter, C.N.: Modification of cysteine residues in the ChlI and ChlH subunits of magnesium chelatase results in enzyme inactivation. Biochem. J., 352, 435–441 (2000)
Willows, R.D.; Beale, S.I.: Heterologous expression of the Rhodobacter capsulatus BchI,-D, and-H genes that encode magnesium chelatase subunits and characterization of the reconstituted enzyme. J. Biol. Chem., 273, 34206–34213 (1998)
Fuesler, T.P.; Wright, L.A., Jr.; Castelfranco, P.A.: Properties of magnesium chelatase in greening etioplasts. Metal ion specificity and effect of substrate concentrations. Plant Physiol., 67, 246–249 (1981)
Nakayama, M.; Masuda, T.; Bando, T.; Yamagata, H.; Ohta, H.; Takamiya, K.: Cloning and expression of the soybean chlH gene encoding a subunit of Mg-chelatase and localization of the Mg2+ concentration-dependent ChlH protein within the chloroplast. Plant Cell Physiol., 39, 275–284 (1998)
Rissler, H.M.; Collakova, E.; DellaPenna, D.; Whelan, J.; Pogson, B.J.: Chlorophyll biosynthesis. Expression of a second Chl I gene of magnesium chelatase in Arabidopsis supports only limited chlorophyll synthesis. Plant Physiol., 128, 770–779 (2002)
Papenbrock, J.; Mock, H.-P.; Tanaka, R.; Kruse, E.; Grimm, B.: Role of magnesium chelatase activity in the early steps of the tetrapyrrole biosynthetic pathway. Plant Physiol., 122, 1161–1169 (2000)
Luo, M.; Weinstein, J.D.; Walker, C.J.: Magnesium chelatase subunit D from pea: characterization of the cDNA, heterologous expression of an enzymatically active protein and immunoassay of the native protein. Plant Mol. Biol., 41, 721–731 (1999)
Papenbrock, J.; Pfundel, E.; Mock, H.-P.; Grimm, B.: Decreased and increased expression of the subunit CHL I diminishes Mg chelatase activity and reduces chlorophyll synthesis in transgenic tobacco plants. Plant J., 22, 155–164 (2000)
Papenbrock, J.; Grafe, S.; Kruse, E.; Hanel, F.; Grimm, B.: Mg-chelatase of tobacco: identification of a Chl D cDNA sequence encoding a third subunit, analysis of the interaction of the three subunits with the yeast two-hybrid system, and reconstitution of the enzyme activity by co-expression of recombinant CHL D, CHL H and CHL I. Plant J., 12, 981–990 (1997)
Willows, R.D.; Gibson, L.C.; Kanangara, C.G.; Hunter, C.N.; von Wettstein, D.: Three separate proteins constitute the magnesium chelatase of Rhodobacter sphaeroides. Eur. J. Biochem., 235, 438–443 (1996)
Lake, V.; Olsson, U.; Willows, R.D.; Hansson, M.: ATPase activity of magnesium chelatase subunit I is required to maintain subunit D in vivo. Eur. J. Biochem., 271, 2182–2188 (2004)
Shepherd, M.; McLean, S.; Hunter, C.N.: Kinetic basis for linking the first two enzymes of chlorophyll biosynthesis. FEBS J., 272, 4532–4539 (2005)
Reid, J.D.; Hunter, C.N.: Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803. J. Biol. Chem., 279, 26893–26899 (2004)
Willows, R.D.; Hansson, A.; Birch, D.; Al-Karadaghi, S.; Hansson, M.: EM single particle analysis of the ATP-dependent BchI complex of magnesium chelatase: an AAA+ hexamer. J. Struct. Biol., 146, 227–233 (2004)
Lake, V.; Willows, R.D.: Rapid extraction of RNA and analysis of transcript levels in Chlamydomonas reinhardtii using real-time RT-PCR: Magnesium chelatase chlH, chlD and chlI gene expression. Photosynth. Res., 77, 69–76 (2003)
Olsson, U.; Sirijovski, N.; Hansson, M.: Characterization of eight barley xantha-f mutants deficient in magnesium chelatase. Plant Physiol. Biochem., 42, 557–564 (2004)
Sirijovski, N.; Olsson, U.; Lundqvist, J.; Al-Karadaghi, S.; Willows, R.D.; Hansson, M.: ATPase activity associated with the magnesium chelatase H-subunit of the chlorophyll biosynthetic pathway is an artefact. Biochem. J., 400, 477–484 (2006)
Jaschke, P.R.; Beatty, J.T.: The photosystem of Rhodobacter sphaeroides assembles with zinc bacteriochlorophyll in a bchD (magnesium chelatase) mutant. Biochemistry, 46, 12491–12500 (2007)
Viney, J.; Davison, P.A.; Hunter, C.N.; Reid, J.D.: Direct measurement of metal-ion chelation in the active site of the AAA(+) ATPase magnesium chelatase. Biochemistry, 46, 12788–12794 (2007)
Ikegami, A.; Yoshimura, N.; Motohashi, K.; Takahashi, S.; Romano, P.G.; Hisabori, T.; Takamiya, K.; Masuda, T.: The CHLI1 subunit of Arabidopsis thaliana magnesium chelatase is a target protein of the chloroplast thioredoxin. J. Biol. Chem., 282, 19282–19291 (2007)
Sawers, R.J.; Farmer, P.R.; Moffett, P.; Brutnell, T.P.: In planta transient expression as a system for genetic and biochemical analyses of chlorophyll biosynthesis. Plant Methods, 2, 15 (2006)
Sawers, R.J.; Viney, J.; Farmer, P.R.; Bussey, R.R.; Olsefski, G.; Anufrikova, K.; Hunter, C.N.; Brutnell, T.P.: The maize Oil yellow1 (Oy1) gene encodes the I subunit of magnesium chelatase. Plant Mol. Biol., 60, 95–106 (2006)
Hedtke, B.; Alawady, A.; Chen, S.; Boernke, F.; Grimm, B.: HEMA RNAi silencing reveals a control mechanism of ALA biosynthesis on Mg chelatase and Fe chelatase. Plant Mol. Biol., 64, 733–742 (2007)
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(2010). Magnesium chelatase. In: Schomburg, D., Schomburg, I., Chang, A. (eds) Class 4–6 Lyases, Isomerases, Ligases. Springer Handbook of Enzymes, vol S7. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-85707-5_138
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DOI: https://doi.org/10.1007/978-3-540-85707-5_138
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