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2. a. Referring to the article "Crystal structure of bacterial succinate:quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE" describe how the chaperone protein SdhE promotes formation of catalytically active succinate:quinone oxidoreductase (SQR) by assisting in the formation of a covalently bound FAD to the SdhA subunit of the enzyme. Refer to figures 6- one paragraph (1) (II) (IV) A C Arg 399 OA HN Arg 399 HN Arg 399 HN O H.O. Arg 399 HN. R287 NH SDHA-H malonate. R390 H* acetate His 45 H CH2 SDHAF2-G78 CH3 N-His 45 CH2 CH3 CH2 Figure 4. The quinone-methide mechanism for autocatalytic covalent flavinylation in complex Il flavoproteins. The amino acid numbering is shown for Escherichia coli SdhA. See details in the text. SdhA, free flavo- protein subunit of E. coli succinate:ubiquinone oxidoreductase. N-His 45 CH3 CH2 His 354 CH3 N-His 45 His 354 B D His 354 His 354 malonate b. Referring to the article, "How an assembly factor enhances covalent FAD attachment to the flavoprotein subunit of complex II" describe the mechanism of attachment of the FAD cofactor. In your answer, discuss how the amino acids shown in figure 4 facilitate covalent attachment of FAD. Identify which polypeptide supplies these amino acids. (one paragraph or bullets) SDHA-R451 FrdA-R390 SdhA-R399 FrdA-R287 OA R451 OA SDHA-R340 H407 SdhA-R286 R340 ---- H296 C. Why is a dicarboxylate ligand needed to initiate flavinylation? (one paragraph referring to figure 7 shown here)

2. a. Referring to the article "Crystal structure of bacterial succinate:quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE" describe how the chaperone protein SdhE promotes formation of catalytically active succinate:quinone oxidoreductase (SQR) by assisting in the formation of a covalently bound FAD to the SdhA subunit of the enzyme. Refer to figures 6- one paragraph (1) (II) (IV) A C Arg 399 OA HN Arg 399 HN Arg 399 HN O H.O. Arg 399 HN. R287 NH SDHA-H malonate. R390 H* acetate His 45 H CH2 SDHAF2-G78 CH3 N-His 45 CH2 CH3 CH2 Figure 4. The quinone-methide mechanism for autocatalytic covalent flavinylation in complex Il flavoproteins. The amino acid numbering is shown for Escherichia coli SdhA. See details in the text. SdhA, free flavo- protein subunit of E. coli succinate:ubiquinone oxidoreductase. N-His 45 CH3 CH2 His 354 CH3 N-His 45 His 354 B D His 354 His 354 malonate b. Referring to the article, "How an assembly factor enhances covalent FAD attachment to the flavoprotein subunit of complex II" describe the mechanism of attachment of the FAD cofactor. In your answer, discuss how the amino acids shown in figure 4 facilitate covalent attachment of FAD. Identify which polypeptide supplies these amino acids. (one paragraph or bullets) SDHA-R451 FrdA-R390 SdhA-R399 FrdA-R287 OA R451 OA SDHA-R340 H407 SdhA-R286 R340 ---- H296 C. Why is a dicarboxylate ligand needed to initiate flavinylation? (one paragraph referring to figure 7 shown here)

Biology: The Dynamic Science (MindTap Course List)
Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Chapter6: Energy, Enzymes, And Biological Reactions
Section: Chapter Questions
Problem 8TYK: Which of the following statements about the allosteric site is true? a. The allosteric site is a...
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a- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5866609/pdf/pnas.201800195.pdf
b- (Article is no longer available)

Here are the articles provided within the question - They are not needed but are available if additional information is warranted - The figures being mentioned are already provided. This is Biochemoistry, please answer each part to the best of your ability. There are a max of 3 parts due to guidelines and please answer each part with clear and efficient work with answers. Thank you

O apo-SdhA III CAP I inactive FBD inefficient E II CAP stabilized in "open" conformation + FAD Sdhe promotes SdhA flavinylation G16, H45 SdhB displaces bound SdhE SdhB holo-SdhA Fig. 6. Proposed SdhA assembly pathway. Path I represents flavinylation of SdhA occurring in the absence of SdhE. In this case, the yield of flavinylated SdhA and hence active SQR is very low. Path Il represents SdhE-assisted flavinylation of SdhA, the optimal route for efficient flavinylation and SQR activity. Path III also represents assembly of SdhA in the absence of SdhE. In this case, however, FAD is absent or remains associated with SdhA noncovalently. This leads to limited progression in the pathway or assembly of a nonfunctional SQR. This model is based largely on the structural (this study) and cellular studies of E. coli SdhA flavinylation and assembly under aerobic conditions. CAP, capping domain of SdhA; FBD, FAD binding domain of SdhA; E, SdhE; G16, Gly16 residue in SdhE; H45, His45 residue in SdhA. FAD is indicated in yellow.
Transcribed Image Text:O apo-SdhA III CAP I inactive FBD inefficient E II CAP stabilized in "open" conformation + FAD Sdhe promotes SdhA flavinylation G16, H45 SdhB displaces bound SdhE SdhB holo-SdhA Fig. 6. Proposed SdhA assembly pathway. Path I represents flavinylation of SdhA occurring in the absence of SdhE. In this case, the yield of flavinylated SdhA and hence active SQR is very low. Path Il represents SdhE-assisted flavinylation of SdhA, the optimal route for efficient flavinylation and SQR activity. Path III also represents assembly of SdhA in the absence of SdhE. In this case, however, FAD is absent or remains associated with SdhA noncovalently. This leads to limited progression in the pathway or assembly of a nonfunctional SQR. This model is based largely on the structural (this study) and cellular studies of E. coli SdhA flavinylation and assembly under aerobic conditions. CAP, capping domain of SdhA; FBD, FAD binding domain of SdhA; E, SdhE; G16, Gly16 residue in SdhE; H45, His45 residue in SdhA. FAD is indicated in yellow.
2. a. Referring to the article "Crystal structure of bacterial succinate:quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE" describe how the chaperone protein SdhE promotes formation of catalytically active succinate:quinone oxidoreductase (SQR) by assisting in the formation of a covalently bound FAD to the SdhA subunit of the enzyme. Refer to figures 6- one paragraph (1) (IV) A с Arg 399 OA HN Arg 399 HN. Arg 399 HN. Arg 399 Way H₂O₂ HN. R287 NH SDHA-H9⁹ malonate R390 His 45 acetate H CH2 CH3 SDHAF2-G78 N-His 45 CH2 CH3 CH2 Figure 4. The quinone-methide mechanism for autocatalytic covalent flavinylation in complex Il flavoproteins. The amino acid numbering is shown for Escherichia coli SdhA. See details in the text. SdhA, free flavo- protein subunit of E. coli succinate:ubiquinone oxidoreductase. N-His 45 CH3 CH2 His 354 CH3 N-His 45 His 354 B D His 354 His 354 malonate b. Referring to the article, "How an assembly factor enhances covalent FAD attachment to the flavoprotein subunit of complex II" describe the mechanism of attachment of the FAD cofactor. In your answer, discuss how the amino acids shown in figure 4 facilitate covalent attachment of FAD. Identify which polypeptide supplies these amino acids. (one paragraph or bullets) SDHA-R451 FrdA-R390 SdhA-R399 FrdA-R287 OA R451 OA SdhA-R286 SDHA-R340 R340 H296 C. Why is a dicarboxylate ligand needed to initiate flavinylation? (one paragraph referring to figure 7 shown here)
Transcribed Image Text:2. a. Referring to the article "Crystal structure of bacterial succinate:quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE" describe how the chaperone protein SdhE promotes formation of catalytically active succinate:quinone oxidoreductase (SQR) by assisting in the formation of a covalently bound FAD to the SdhA subunit of the enzyme. Refer to figures 6- one paragraph (1) (IV) A с Arg 399 OA HN Arg 399 HN. Arg 399 HN. Arg 399 Way H₂O₂ HN. R287 NH SDHA-H9⁹ malonate R390 His 45 acetate H CH2 CH3 SDHAF2-G78 N-His 45 CH2 CH3 CH2 Figure 4. The quinone-methide mechanism for autocatalytic covalent flavinylation in complex Il flavoproteins. The amino acid numbering is shown for Escherichia coli SdhA. See details in the text. SdhA, free flavo- protein subunit of E. coli succinate:ubiquinone oxidoreductase. N-His 45 CH3 CH2 His 354 CH3 N-His 45 His 354 B D His 354 His 354 malonate b. Referring to the article, "How an assembly factor enhances covalent FAD attachment to the flavoprotein subunit of complex II" describe the mechanism of attachment of the FAD cofactor. In your answer, discuss how the amino acids shown in figure 4 facilitate covalent attachment of FAD. Identify which polypeptide supplies these amino acids. (one paragraph or bullets) SDHA-R451 FrdA-R390 SdhA-R399 FrdA-R287 OA R451 OA SdhA-R286 SDHA-R340 R340 H296 C. Why is a dicarboxylate ligand needed to initiate flavinylation? (one paragraph referring to figure 7 shown here)
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