Contribution of arginine (HC3) 141α to the Bohr effect of the fourth binding step in the reaction of ligand with human hemoglobin
A few years ago we reported that histidine (HC3) 146β plays a major role in the pH‐dependent propeties of the R‐state of human hemoglobin, accounting for close to 50% of the R‐state Bohr effect. We have extended these studies by examining the role of arginine 141α, another group known to affect the...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1987, Vol.2 (1), p.72-77 |
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| container_title | Proteins, structure, function, and bioinformatics |
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| creator | Kwiatkowski, Laura D. Noble, Robert W. |
| description | A few years ago we reported that histidine (HC3) 146β plays a major role in the pH‐dependent propeties of the R‐state of human hemoglobin, accounting for close to 50% of the R‐state Bohr effect. We have extended these studies by examining the role of arginine 141α, another group known to affect the overall Bohr effect. We have compared the pH dependencies of the rate constants for the dissociation and combination of the fourth carbon monoxide molecule, I4 and I′4, respectively, for native hemoglobin A (HbA) and a control reconstututed HbA, and des‐(Arg 141α) HbA, the hemoglobin molecule resulting from the enzymatic removal of the C–terminal arginine of the α‐chain of human Hb. From these kinetic contants the pH dependence of L4, by about 80% between pH 6 and 8, where the aldkaline Bohr effect normally occurs, The sum of the effects of the removal of His 146β and of Arg 141α is grater than 100%. This suggests that at least one of these modifications altrs the contrubutions of other residues of this Bohr effect. |
| doi_str_mv | 10.1002/prot.340020109 |
| format | Article |
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We have extended these studies by examining the role of arginine 141α, another group known to affect the overall Bohr effect. We have compared the pH dependencies of the rate constants for the dissociation and combination of the fourth carbon monoxide molecule, I4 and I′4, respectively, for native hemoglobin A (HbA) and a control reconstututed HbA, and des‐(Arg 141α) HbA, the hemoglobin molecule resulting from the enzymatic removal of the C–terminal arginine of the α‐chain of human Hb. From these kinetic contants the pH dependence of L4, by about 80% between pH 6 and 8, where the aldkaline Bohr effect normally occurs, The sum of the effects of the removal of His 146β and of Arg 141α is grater than 100%. This suggests that at least one of these modifications altrs the contrubutions of other residues of this Bohr effect.</description><identifier>ISSN: 0887-3585</identifier><identifier>EISSN: 1097-0134</identifier><identifier>DOI: 10.1002/prot.340020109</identifier><identifier>PMID: 3447169</identifier><identifier>CODEN: PSFGEY</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Arginine ; Biological and medical sciences ; Carbon Monoxide - metabolism ; CO equilibrium constants ; des-(Arg 141α)HbA ; Fundamental and applied biological sciences. Psychology ; heme proteins ; hemoglobin ; Hemoglobin A - metabolism ; high-affinity state ; Humans ; Hydrogen-Ion Concentration ; Interactions. Associations ; Intermolecular phenomena ; Kinetics ; ligand binding ; ligands ; man ; Models, Chemical ; Molecular biophysics ; Protein Conformation</subject><ispartof>Proteins, structure, function, and bioinformatics, 1987, Vol.2 (1), p.72-77</ispartof><rights>Copyright © 1987 Alan R. Liss, Inc.</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3539-1bcafee616ee87496bf9d8fcd9db2e9302f9f30962ed40282d0b0ed57076b6643</citedby><cites>FETCH-LOGICAL-c3539-1bcafee616ee87496bf9d8fcd9db2e9302f9f30962ed40282d0b0ed57076b6643</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fprot.340020109$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fprot.340020109$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,4010,27900,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7575966$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3447169$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kwiatkowski, Laura D.</creatorcontrib><creatorcontrib>Noble, Robert W.</creatorcontrib><title>Contribution of arginine (HC3) 141α to the Bohr effect of the fourth binding step in the reaction of ligand with human hemoglobin</title><title>Proteins, structure, function, and bioinformatics</title><addtitle>Proteins</addtitle><description>A few years ago we reported that histidine (HC3) 146β plays a major role in the pH‐dependent propeties of the R‐state of human hemoglobin, accounting for close to 50% of the R‐state Bohr effect. We have extended these studies by examining the role of arginine 141α, another group known to affect the overall Bohr effect. We have compared the pH dependencies of the rate constants for the dissociation and combination of the fourth carbon monoxide molecule, I4 and I′4, respectively, for native hemoglobin A (HbA) and a control reconstututed HbA, and des‐(Arg 141α) HbA, the hemoglobin molecule resulting from the enzymatic removal of the C–terminal arginine of the α‐chain of human Hb. From these kinetic contants the pH dependence of L4, by about 80% between pH 6 and 8, where the aldkaline Bohr effect normally occurs, The sum of the effects of the removal of His 146β and of Arg 141α is grater than 100%. This suggests that at least one of these modifications altrs the contrubutions of other residues of this Bohr effect.</description><subject>Arginine</subject><subject>Biological and medical sciences</subject><subject>Carbon Monoxide - metabolism</subject><subject>CO equilibrium constants</subject><subject>des-(Arg 141α)HbA</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>heme proteins</subject><subject>hemoglobin</subject><subject>Hemoglobin A - metabolism</subject><subject>high-affinity state</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Interactions. Associations</subject><subject>Intermolecular phenomena</subject><subject>Kinetics</subject><subject>ligand binding</subject><subject>ligands</subject><subject>man</subject><subject>Models, Chemical</subject><subject>Molecular biophysics</subject><subject>Protein Conformation</subject><issn>0887-3585</issn><issn>1097-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAQhi0EKkvhyg3JB4TgkMWOHTs-0hW0QNUCWgQ3y0nGu4bEXuxEpVfeiBfhmfB2lxW3XmzL8_3_jOZH6DElc0pI-XITwzhnPD8JJeoOmuVTFoQyfhfNSF3LglV1dR89SOkbIUQoJo7QEeNcUqFm6Nci-DG6Zhpd8DhYbOLKeecBPz9bsBeYcvrnNx4DHteAT8I6YrAW2nGLbr9smOK4xo3znfMrnEbYYOdvShFM-8-1dyvjO3zlMrueBuPxGoaw6kMWPkT3rOkTPNrfx-jzm9fLxVlxfnn6dvHqvGhZxVRBm9ZYAEEFQC25Eo1VXW3bTnVNCYqR0irLiBIldJyUddmRhkBXSSJFIwRnx-jZzjev7McEadSDSy30vfEQpqRlnddDhbgVpFxWJNtmcL4D2xhSimD1JrrBxGtNid6mo7fp6EM6WfBk7zw1A3QHfB9Hrj_d101qTW-j8a1LB0xWslI3A6odduV6uL6lqf7w6XL5_wjFTutyVj8PWhO_ayGZrPSXi1P9dfn-47uTC64p-wsFDLjT</recordid><startdate>1987</startdate><enddate>1987</enddate><creator>Kwiatkowski, Laura D.</creator><creator>Noble, Robert W.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>1987</creationdate><title>Contribution of arginine (HC3) 141α to the Bohr effect of the fourth binding step in the reaction of ligand with human hemoglobin</title><author>Kwiatkowski, Laura D. ; Noble, Robert W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3539-1bcafee616ee87496bf9d8fcd9db2e9302f9f30962ed40282d0b0ed57076b6643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Arginine</topic><topic>Biological and medical sciences</topic><topic>Carbon Monoxide - metabolism</topic><topic>CO equilibrium constants</topic><topic>des-(Arg 141α)HbA</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>heme proteins</topic><topic>hemoglobin</topic><topic>Hemoglobin A - metabolism</topic><topic>high-affinity state</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Interactions. Associations</topic><topic>Intermolecular phenomena</topic><topic>Kinetics</topic><topic>ligand binding</topic><topic>ligands</topic><topic>man</topic><topic>Models, Chemical</topic><topic>Molecular biophysics</topic><topic>Protein Conformation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kwiatkowski, Laura D.</creatorcontrib><creatorcontrib>Noble, Robert W.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Proteins, structure, function, and bioinformatics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kwiatkowski, Laura D.</au><au>Noble, Robert W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Contribution of arginine (HC3) 141α to the Bohr effect of the fourth binding step in the reaction of ligand with human hemoglobin</atitle><jtitle>Proteins, structure, function, and bioinformatics</jtitle><addtitle>Proteins</addtitle><date>1987</date><risdate>1987</risdate><volume>2</volume><issue>1</issue><spage>72</spage><epage>77</epage><pages>72-77</pages><issn>0887-3585</issn><eissn>1097-0134</eissn><coden>PSFGEY</coden><abstract>A few years ago we reported that histidine (HC3) 146β plays a major role in the pH‐dependent propeties of the R‐state of human hemoglobin, accounting for close to 50% of the R‐state Bohr effect. We have extended these studies by examining the role of arginine 141α, another group known to affect the overall Bohr effect. We have compared the pH dependencies of the rate constants for the dissociation and combination of the fourth carbon monoxide molecule, I4 and I′4, respectively, for native hemoglobin A (HbA) and a control reconstututed HbA, and des‐(Arg 141α) HbA, the hemoglobin molecule resulting from the enzymatic removal of the C–terminal arginine of the α‐chain of human Hb. From these kinetic contants the pH dependence of L4, by about 80% between pH 6 and 8, where the aldkaline Bohr effect normally occurs, The sum of the effects of the removal of His 146β and of Arg 141α is grater than 100%. This suggests that at least one of these modifications altrs the contrubutions of other residues of this Bohr effect.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>3447169</pmid><doi>10.1002/prot.340020109</doi><tpages>6</tpages></addata></record> |
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| ispartof | Proteins, structure, function, and bioinformatics, 1987, Vol.2 (1), p.72-77 |
| issn | 0887-3585 1097-0134 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Arginine Biological and medical sciences Carbon Monoxide - metabolism CO equilibrium constants des-(Arg 141α)HbA Fundamental and applied biological sciences. Psychology heme proteins hemoglobin Hemoglobin A - metabolism high-affinity state Humans Hydrogen-Ion Concentration Interactions. Associations Intermolecular phenomena Kinetics ligand binding ligands man Models, Chemical Molecular biophysics Protein Conformation |
| title | Contribution of arginine (HC3) 141α to the Bohr effect of the fourth binding step in the reaction of ligand with human hemoglobin |
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