1. Volume 2, Issue 3, Pages 407-415 (May 2009)
The Interaction of Spinach Nitrite Reductase with Ferredoxin: A Site-Directed Mutation Study 
Hirasawa Masakazu , Tripathy Jatindra N. , Somasundaram Ramasamy , Johnson Michael K. , Bhalla Megha , Allen James P. , Knaff David B.  
Molecular Plant 
Volume 2, Issue 3, Pages (May 2009)
DOI: /mp/ssn098
Copyright © 2009 The Authors. All rights reserved. Terms and Conditions

2. Figure 1 A Proposed Model for the NiR–Fd Complex.
Shown are the protein backbones of nitrite reductase (yellow) and ferredoxin (pink), the three cofactors: siroheme (atom type), two iron–sulfur clusters (gold and pink). From nitrite reductase (blue, regular labels), the following amino acids involved in the binding site are shown: Lys 49, Lys 80, Lys 83, Lys 100, Lys 268, Asn 304, and Arg 502. Three other residues (red, regular labels), Arg 375, Lys 436, and Arg 55, have been altered in this study but are removed from the putative binding site. Note that Arg 375 is a surface residue but relatively close to the siroheme and iron–sulfur cluster. For spinach ferredoxin, shown are three amino acid residues, which are near the proposed binding site and have been altered in this study (green, bold labels): Phe 63, Glu 92, and Glu 93, which correspond to Phe 65, Glu 93, and Glu 94 in Anabaena ferredoxin. The structural models are 2AKJ (nitrite reductase, Swamy et al., 2005) and 1A70 (spinach ferredoxin; mutant with Glu 92 changed to Lys, Binda et al. 1998).
Molecular Plant 2009 2, DOI: ( /mp/ssn098)
Copyright © 2009 The Authors. All rights reserved. Terms and Conditions

3. Figure 2
X-Band EPR Spectra of Cyanide-Bound Wild-Type and Variant Forms of His-Tagged Recombinant Spinach Nitrite Reductase.
Samples were treated with a 10-fold molar excess of KCN in 250 mM potassium phosphate buffer at pH 7.5. EPR spectra were recorded at 15 K with a microwave power of 2 mW, a microwave frequency of 9.604 GHz, and a modulation amplitude of 6.4 Gauss.
Molecular Plant 2009 2, DOI: ( /mp/ssn098)
Copyright © 2009 The Authors. All rights reserved. Terms and Conditions

4. Figure 3
X-Band EPR Spectra of Dithionite-Reduced Cyanide-Bound Wild-Type and Variant Forms of His-Tagged Recombinant Spinach Nitrite Reductase.
The cyanide-bound nitrite reductase samples described in Figure 2 were anaerobically reduced using a 10-fold molar excess of sodium dithionite. EPR spectra were recorded at 15 K with a microwave power of 2 mW, a microwave frequency of 9.604 GHz, and a modulation amplitude of 6.4 Gauss.
Molecular Plant 2009 2, DOI: ( /mp/ssn098)
Copyright © 2009 The Authors. All rights reserved. Terms and Conditions