dpor subunit n  (Marinus)

Journal: Nature Catalysis

Article Title: Methylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage

doi: 10.1038/s41929-025-01426-2

Figure Lengend Snippet: a , A schematic overview illustrating structures from key nitrogenase and Nfl proteins with their associated metalloclusters responsible for electron transfer and catalysis. Electrons are sequentially transferred through transient interaction of the homodimeric reductase components to the metal cofactors of the heterotetrameric catalytic components. All reductase components harbour an [Fe S ]-cluster, which donates electrons to the subunit bridging metallocofactor of the catalytic component. For the DPOR (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site . In DPOR, the substrate protochlorophyllide a (Pchlide) sits directly at the active site , . Nitrogenases harbour more complex metalloclusters in their active sites, such as FeMoco , and Nif(EN) 2 harbours the [Fe 8 S 9 C]-cluster . The metallocluster composition for the methylthio-alkane reductase as well as the stoichiometry of the reaction was still unresolved. The protein name of each subunit is shown and derived from the corresponding gene name. Genes for each nitrogenase(-like) enzyme are usually organized in an individual operon encoding the subunits of reductase and catalytic components. Not shown here is the very distant homologue Ni 2+ -sirohydrochlorin a , c -diamide reductase (CfbD), which catalyses the second last step of coenzyme F 430 biosynthesis, a tetrapyrrole cofactor in methanogens . b , Main catalytic reactions. DPOR reduces the C17=C18 double bond of Pchlide to chlorophyllide a (Chlide) in the chlorophyll a biosynthetic pathway , . The Nif(EN) 2 maturase converts the precursor [Fe 8 S 9 C]-cluster into FeMoco by inserting Mo and ( R )-homocitrate . Mo-nitrogenase reduces protons and N 2 to NH 3 and H 2 (ref. ). The methylthio-alkane reductase is proposed to reduce MT-EtOH to methanethiol and C 2 H (ref. ). Protein phylogenetic relationships are depicted based on Extended Data Fig. . c , Legend of the metalloclusters found in nitrogenase and Nfl proteins shown in a .

Article Snippet: For the DPOR (Bch(NB) 2 ) and FeMoco maturase Nif(EN) 2 , this is an [Fe S ]-cluster , , while the Mo-nitrogenase catalytic component (Nif(DK) 2 ) harbours a P-cluster ([Fe 8 S 7 ]-cluster) as an electron relay to the active site .

Techniques: Derivative Assay

Journal: Journal of structural and functional genomics

Article Title: Solution NMR structures provide first structural coverage of the large protein domain family PF08369 and complementary structural coverage of dark operative protochlorophyllide oxidoreductase complexes

doi: 10.1007/s10969-013-9159-5

Figure Lengend Snippet: a The (BchN-BchB)2 from R. capsulatus (PDB ID: 3AEK) was superimposed on the (BchN-BchB)2 unit of P. marinus DPOR complex (PDB ID: 2YNM) and is shown as a space filling representation colored according to scores from PredUs prediction for regions potentially involved in protein-protein interaction (residues with scores larger than zero are shown from light red to red with increasing score; see Fig. S7). The patches labeled with ‘P1’ are close to Pchlide binding site and might interact with the PCP-red domains at different stages of the catalytic cycle (see text). The PCP-red domains of the P. marinus DPOR complex are displayed as ribbon drawings colored in gold, while other domains in the structure of the P. marinus DPOR complex are in gray. b Ribbon representation of the lowest energy conformer of BchB(484-537) (PDB ID: 2KRU; α-helices and β-sheet are represented in blue and cyan respectively) superimposed on crystal structure of PCP-red domain from P. marinus (2YNM, chain D; gold). The structures were superimposed according to DALI alignment by minimizing the RMSD of the Cα atoms of the following residues: 490-497, 501-517, 525-534 of BchB(484-537) and 483-490, 494-510, 518-527 of P. marinus PCP-red domain. c Comparison of the backbone dihedral angels φ and ψ observed in the BchB(484-537) solution NMR structure and the P. marinus PCP-red domain structure. The values of the ensemble of NMR conformers are shown in blue with boxes drawn around the observed range, and the values observed in the crystal structure are shown in red. While the polypeptide segment corresponding to β-strand I in BchB(484-537) is likewise in an extended conformation in the P. marinus PCP-red domain, this is not the case for the segment corresponding to β-strand I in BchB(484-537). The amino acid residue numberings for BchB(484-537) and the PCP-red domain from P. marinus are provided in black (bottom) and red (top), respectively.

Article Snippet: The PCP-red domains of the P . marinus DPOR complex are displayed as ribbon drawings colored in gold, while other domains in the structure of the P . marinus DPOR complex are in gray. b Ribbon representation of the lowest energy conformer of BchB(484-537) (PDB ID: 2KRU; α-helices and β-sheet are represented in blue and cyan respectively) superimposed on crystal structure of PCP-red domain from P . marinus (2YNM, chain D; gold).

Techniques: Labeling, Binding Assay, Comparison, Residue

Journal: The Journal of Biological Chemistry

Article Title: Chimeric Nitrogenase-like Enzymes of (Bacterio)chlorophyll Biosynthesis *

doi: 10.1074/jbc.M901331200

Figure Lengend Snippet: TABLE 1

Article Snippet: Chimeric DPOR Enzymes Are Active Six chimeric DPOR enzymes, consisting of individual subunits from C. tepidum, P. marinus , and T. elongatus , were reconstituted under the conditions of the DPOR standard assay.

Techniques: Sequencing

Journal: The Journal of Biological Chemistry

Article Title: Chimeric Nitrogenase-like Enzymes of (Bacterio)chlorophyll Biosynthesis *

doi: 10.1074/jbc.M901331200

Figure Lengend Snippet: TABLE 1

Article Snippet: Six chimeric DPOR enzymes, consisting of individual subunits from C. tepidum, P. marinus , and T. elongatus , were reconstituted under the conditions of the DPOR standard assay.

Techniques: Sequencing