NDLI: Identification of the Binding Region of the [2Fe-2S] Ferredoxin in Stearoyl-Acyl Carrier Protein Desaturase

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Structural Perturbations in the Ala → Val Polymorphism of Methylenetetrahydrofolate Reductase: How Binding of Folates May Protect against Inactivation† ‡

Identification of the Binding Region of the [2Fe-2S] Ferredoxin in Stearoyl-Acyl Carrier Protein Desaturase

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Rhodopsin Photointermediates in 2D Crystals at Physiological Temperatures

Peroxidase Activity and Structural Transitions of Cytochrome c Bound to Cardiolipin-Containing Membranes

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Identification of the Binding Region of the [2Fe-2S] Ferredoxin in Stearoyl-Acyl Carrier Protein Desaturase

Content Provider	PubMed Central
Author	Sobrado, Pablo Lyle, Karen S. Kaul, Steven P. Turco, Michelle M. Arabshahi, Ida Marwah, Ashok Fox, Brian G.
Abstract	Stearoyl-acyl carrier protein desaturase (Δ9D) catalyzes the O2 and 2e- dependent desaturation of stearoyl-acyl carrier protein (18:0-ACP) to yield oleoyl-ACP (18:1-ACP). The 2e- are provided by essential interactions with reduced plant-type [2Fe-2S] ferredoxin (Fd). We have investigated the protein-protein interface involved in the Fd-Δ9D complex by use of chemical cross-linking, site-directed mutagenesis, steady-state kinetic approaches and molecular docking studies. Treatment of the different proteins with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide and N-hydroxysuccinimide revealed that carboxylate residues from Fd and lysine residues from Δ9D contribute to the cross-linking. The single substitutions of K60A, K56A, and K230A on Δ9D decreased the k cat/K M for Fd by 4-, 22- and 2,400-fold, respectively, as compared to wt Δ9D and a K41A substitution. The double substitution K56A/K60A decreased the k cat/K M for Fd by 250-fold, while the triple mutation K56A/K60A/K230A decreased the k cat/K M for Fd by at least 700,000-fold. These results strongly implicate the triad of K56, K60 and K230 of Δ9D in the formation of a catalytic complex with Fd. Molecular docking studies indicate that electrostatic interactions between K56 and K60 and carboxylate groups on Fd may situate the [2Fe-2S] cluster of Fd near to W62, a surface residue that is structurally conserved in both ribonucleotide reductase and mycobacterial putative acyl-ACP desaturase DesA2. Owing to the considerably larger effects on catalysis, K230 appears to have other contributions to catalysis arising from its positioning in helix-7 and its close spatial location to the diiron center ligands E229 and H232. These results are considered in the light of the presently available models for Fd-mediated electron transfer in Δ9D and other protein-protein complexes.
Related Links	http://dx.doi.org/10.1021/bi0600547
Ending Page	4858
Page Count	11
Starting Page	4848
File Format	PDF
ISSN	00062960
e-ISSN	15204995
Journal	Biochemistry
Issue Number	15
Volume Number	45
Language	English
Publisher Date	2006-04-01
Access Restriction	Open
Subject Keyword	Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry

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Identification of the Binding Region of the [2Fe-2S] Ferredoxin in Stearoyl-Acyl Carrier Protein Desaturase: Insight into the Catalytic Complex and Mechanism of Action

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Primary structures of the precursor and mature forms of stearoyl-acyl carrier protein desaturase from safflower embryos and requirement of ferredoxin for enzyme activity.

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Identification of the Binding Region of the [2Fe-2S] Ferredoxin in Stearoyl-Acyl Carrier Protein Desaturase

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