a- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5866609/pdf/pnas.201800195.pdfb- (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 Oapo-SdhAIIICAPIinactiveFBDinefficientEIICAP stabilized in"open" conformation+ FADSdhe promotesSdhA flavinylationG16,H45SdhB displacesbound SdhESdhBholo-SdhAFig. 6. Proposed SdhA assembly pathway. Path I represents flavinylation of SdhA occurring in the absence of SdhE. In this case, the yield of flavinylated SdhAand hence active SQR is very low. Path Il represents SdhE-assisted flavinylation of SdhA, the optimal route for efficient flavinylation and SQR activity. Path IIIalso represents assembly of SdhA in the absence of SdhE. In this case, however, FAD is absent or remains associated with SdhA noncovalently. This leads tolimited 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. coliSdhA flavinylation and assembly under aerobic conditions. CAP, capping domain of SdhA; FBD, FAD binding domain of SdhA; E, SdhE; G16, Gly16 residue inSdhE; H45, His45 residue in SdhA. FAD is indicated in yellow. 2. a.Referring to the article "Crystal structure of bacterial succinate:quinone oxidoreductaseflavoprotein SdhA in complex with its assembly factor SdhE" describe how the chaperone protein SdhEpromotes formation of catalytically active succinate:quinone oxidoreductase (SQR) by assisting in theformation of a covalently bound FAD to the SdhA subunit of the enzyme. Refer to figures 6- one paragraph(1)(IV)AсArg 399OAHNArg 399HN.Arg 399HN.Arg 399WayH₂O₂HN.R287NHSDHA-H9⁹malonateR390His 45acetateHCH2CH3SDHAF2-G78N-His 45CH2CH3CH2Figure 4. The quinone-methide mechanism for autocatalytic covalentflavinylation in complex Il flavoproteins. The amino acid numbering isshown for Escherichia coli SdhA. See details in the text. SdhA, free flavo-protein subunit of E. coli succinate:ubiquinone oxidoreductase.N-His 45CH3CH2His 354CH3N-His 45His 354BDHis 354His 354malonateb.Referring to the article, "How an assembly factorenhances covalent FAD attachment to the flavoprotein subunit ofcomplex II" describe the mechanism of attachment of the FADcofactor. In your answer, discuss how the amino acids shown infigure 4 facilitate covalent attachment of FAD. Identify whichpolypeptide supplies these amino acids. (one paragraph or bullets)SDHA-R451FrdA-R390SdhA-R399FrdA-R287OAR451OASdhA-R286SDHA-R340R340H296C.Why is a dicarboxylate ligandneeded to initiate flavinylation? (one paragraphreferring to figure 7 shown here)

Here we are concerned about the bacterial SQR (Succinate Quinone Oxidoreductase) protein. Bacterial…

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)

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P