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Autor
Filipiak Marian
Tytuł
Hydrogenase from Megasphaera elsdenii
Hydrogenase from Megasphaera elsdenii
Źródło
Zeszyty Naukowe. Seria 2, Prace Habilitacyjne / Akademia Ekonomiczna w Poznaniu, 1996, nr 146, 82 s., bibliogr. 175 poz.
Słowa kluczowe
Związki chemiczne, Biochemia, Mikrobiologia, Biologia, Badania towaroznawcze, Chemia spożywcza
Chemical compounds, Biochemistry, Microbiology, Biology, Commodity research, Food chemistry
Uwagi
summ., streszcz.
Abstrakt
Hydrogenazy są to enzymy katalizujące odwracalny proces utleniania wodoru. W pierwszym rozdziale swojej pracy przedstawiłem charakterystykę biochemiczną i spektroskopową tych enzymów. Hydrogenazy izolowane z różnych mikroorganizmów, a nawet różnych szczepów tych samych mikroorganizmów wykazują odmienną budowę, aktywność właściwą wyrażaną zarówno jako szybkość wytwarzania wodoru jak i szybkość jego utleniania, specyficzność w stosunku do nośnika elektronów, wrażliwość na działanie tlenu. Jedyną wspólną cechą hydrogenaz jest to, że zawierają one skupiska żelazowo-siarkowe. Poza tym w skład centrum katalitycznego większości hydrogenaz wchodzi nikiel, a tylko niewielka ich część zawiera żelazo jako jedyny metal. Do tej ostatniej grupy zalicza się m.in. trzy hydrogenazy o bardzo zbliżonych właściwościach, pochodzące z Desulfovibrio vulgaris, Clostridium pasteurianum i Megasphaera elsdenii. W II rozdziale pracy przedstawiłem wyniki swoich badań nad hydrogenazą z Megasphaera elsdenii. Enzym ten oczyściłem do stanu jednorodnego przy zastosowaniu w ostatnim etapie chromatografii FPLC. Otrzymane białko enzymatyczne w procesie elektroforezy na żelu poliakryloamidowym w obecności siarczanu dodecylu pojawia się jako pojedyncze pasmo o masie cząsteczkowej 57-59 kDa. W swojej pracy przedstawiłem dowody na to, że rozpuszczalna frakcja z komórek bakterii M. elsdenii nie zawiera drugiej hydrogenazy, jak to sugerowano w literaturze. Przy pomocy wirówki analityczne j porównałem właściwości hydrodynamiczne hydrogenazy z M. elsdenii i hydrogenazy z D. vulgaris (Hildenborough) złożonej z dwóch podjednostek. Szybkość przesuwania granicy faz w ultrawirówce była rejestrowana przez pomiar absorpcji wywołanej obecnością w cząsteczkach tych enzymów skupisk żelazowo-siarkowych. Pomiary szybkości sedymentacji wykazały, że enzym z M. elsdenii ma prawdopodobnie kształt globularny, podczas gdy cząsteczka enzymu z D. vulgaris jest mniej symetryczna. Masa cząsteczkowa hydrogenazy z M. elsdenii wyznaczona w pomiarach równowagi sedymentacyjnej przeprowadzonych w różnych warunkach wynosi 58 kDa, zaś hydrogenazy z D. vulgaris 54 kDa. Oczyszczona hydrogenaza z M. elsdenii o maksymalnej aktywności charakteryzuje się stosunkiem absorbancji A405/A280 równym 0,36 oraz aktywnością właściwą wyrażoną w szybkości wytwarzania wodoru równą 400 µmoli H2 • min-1 • (mg białka)-1 w temp. 30° C i pH 8,0. Stwierdziłem, że enzym zawiera 13-18 atomów żelaza i siarki w monomerycznej cząsteczce o masie 58 kDa. Badanie przy pomocy spektroskopii elektronowego rezonansu paramagnetycznego enzymu w formie zredukowanej wodorem doprowadziło do wniosku, że 8 jonów żelaza wchodzi w skład dwóch skupisk żelazowo-siarkowych zdolnych do przenoszenia 2 elektronów. Skupiska te, podobnie jak w bakteryjnej ferredoksynie mają kształt regularnych sześcianów zawierających po 4 jony żelaza i siarki. Utlenienie enzymu prowadzi do powstania nowego sygnału EPR charakterystycznego dla układu o S = 1/2 pochodzącego prawdopodobnie od pozostałych jonów żelaza wchodzących w skład aktywnego centrum enzymu. Szybkość wytwarzania wodoru, zawartość żelaza oraz intensywność sygnału EPR enzymu utlenionego są wyraźnie skorelowane. Wyniki moich badań wskazują na to, że oczyszczona hydrogenaza istnieje w postaci mieszaniny w pełni aktywnego holoenzymu i białka nieaktywnego. To ostatnie posiada nadal w swojej cząsteczce dwa skupiska żelazowo-siarkowe w postaci sześcianów, lecz jest pozbawione żelaza wchodzącego w skład centrum aktywnego. Zbadałem również kinetykę reakcji przenoszenia elektronu między hydrogenazą a dwoma nośnikami elektronów. Przy pomocy cyklicznej woltametrii wyznaczyłem stałe szybkości reakcji drugiego rzędu zachodzącej między enzymem a ferredoksyną i rubredoksyną z M. elsdenii. Wynoszą one 3,9 • 106 M-1 • s-1 dla ferredoksyny i 1,23 • 106 M-1 • s-1 dla rubredoksyny. Z tych danych wynika, że szybkość przenoszenia elektronu z udziałem tych nośników jest bardzo wysoka. Sugeruje to, że nie tylko ferredoksyna, ale także rubredoksyna jest naturalnym nośnikiem elektronów dla hydrogenazy z M. elsdenii. (abstrakt oryginalny)

Hydrogenases are enzymes that catalyze the reversible oxidation of molecular hydrogen. In the first chapter of this thesis I present biochemical and spectroscopic properties of these enzymes. When isolated from different microorganisms, and even different strains, hydrogenases diverge in molecular composition, specific activity in H2 production and H2 oxidation, electron carrier specificity, sensitivity to inactivation by oxygen. Their only common feature is that they are iron-sulfur proteins. Most of hydrogenases contain nickel in the catalytic center and a few of them are known that lack nickel and contain iron as the only metallic element. In the latter group three hydrogenases appear to form a small subgroup of closely related entities. These are enzymes from Clostridium pasteurianum, Desulfovibrio vulgaris and Megasphaera elsdenii. In the second chapter of this thesis I present my data on the hydrogenase from Megasphaera elsdenii. I have purified this hydrogenase to homogeneity using an FPLC procedure as the final step. The protein gives a single band in SDS/PAGE with an apparent molecular mass of 57-59 kDa. I have proved that there is no second hydrogenase activity in the soluble fraction of M. elsdenii what has been suggested in literature. I compared the hydrodynamics of the hydrogenase from Megasphaera elsdenii to the two-subunit Fe hydrogenase from Desulfovibrio vulgaris (Hildenborough) in the analytical ultracentrifuge using the absorption of the intrinsic iron sulfur clusters as the monitor. Sedimentation-velocity experiments indicate the M. elsdeniienzyme to be essentially globular, while the D. vulgaris enzyme has a less symmetric shape. From sedimentation equilibrium measurements under different conditions I calculated an enzyme average molecular mass of 58 kDa (M. elsdenii) and 54 kDa (D. vulgaris). Pure, maximally active M. elsdenii hydrogenase has A405/A280 ratio equal to 0,36 and a specific H2-production activity of 400 μmol H2 • min-1 • (mg protein) -1 at 30°C and pH 8.0. According to my data the enzyme contains some 13-18 iron and acid-labile sulfur ions per 58-kDa monomer. Eight of these Fe-S are present as two electron-transferring ferredoxin-like cubanes as indicated by pH-dependent EPR spectroscopy on the H2-reduced enzyme. In the (re)oxidized state the remainder iron gives rise to a novel single S = 1/2 EPR signal. This signal is probably associated with the enzyme active site. Hydrogen-production activity, content of remainder iron and intensity of EPR signal of reoxidized enzyme are mutually correlated. The results of my study lead to the conclusion that purified hydrogenase appears to exist as a mixture of fully active holoenzyme and inactive protein still carrying the two cubanes but deficient in active site iron. Using cyclic voltammetry I investigated the electron transfer kinetics between the hydrogenase from Megasphaera elsdenii and two electron carriers. The second-order rate constants for electron transfer between the enzyme and rubredoxin and ferredoxin from Megasphaera elsdenii are 1.23 • 106 and 3.9 • 106 M-1 s-1, respectively. Thus, both electron carriers show a very efficient electron transfer what suggests that not only ferredoxin but also rubredoxin is a natural electron carrier for the hydrogenase from Megasphaera elsdenii. (original abstract)
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Bibliografia
Pokaż
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